Serpins are a superfamily of proteins with similar structures that were first re

cognized for their protease inhibition activity and are found in all kingdoms of
life. Their unusual mechanism of action irreversibly inhibits their target prot
ease by undergoing a large conformational change to disrupt its active site. Thi
s contrasts with the more common competitive mechanism for protease inhibitors t
hat bind to and block access to the protease active site. Protease inhibition by
serpins controls an array of biological processes, including coagulation and in
flammation, and consequently these proteins are the target of medical research.
Their conformational-change mechanism confers certain advantages, but it also ha
s drawbacks: serpins are vulnerable to mutations that can result in protein misf
olding and the formation of inactive long-chain polymers. Serpin polymerization
not only reduces the amount of active inhibitor, but also leads to accumulation
of the polymers, which can cause cell death and even organ failure. (Serpins are
a superfamily of proteins with similar structures that were first recognized fo
r their protease inhibition activity and are found in all kingdoms of life. Thei
r unusual mechanism of action irreversibly inhibits their target protease by und
ergoing a large conformational change to disrupt its active site. This contrasts
with the more common competitive mechanism for protease inhibitors that bind to
and block access to the protease active site. Protease inhibition by serpins co
ntrols an array of biological processes, including coagulation and inflammation,
and consequently these proteins are the target of medical research. Their confo
rmational-change mechanism confers certain advantages, but it also has drawbacks
: serpins are vulnerable to mutations that can result in protein misfolding and
the formation of inactive long-chain polymers. Serpin polymerization not only re
duces the amount of active inhibitor, but also leads to accumulation of the poly
mers, which can cause cell death and even organ failure. (Serpins are a superfam
ily of proteins with similar structures that were first recognized for their pro
tease inhibition activity and are found in all kingdoms of life. Their unusual m
echanism of action irreversibly inhibits their target protease by undergoing a l
arge conformational change to disrupt its active site. This contrasts with the m
ore common competitive mechanism for protease inhibitors that bind to and block
access to the protease active site. Protease inhibition by serpins controls an a
rray of biological processes, including coagulation and inflammation, and conseq
uently these proteins are the target of medical research. Their conformational-c
hange mechanism confers certain advantages, but it also has drawbacks: serpins a
re vulnerable to mutations that can result in protein misfolding and the formati
on of inactive long-chain polymers. Serpin polymerization not only reduces the a
mount of active inhibitor, but also leads to accumulation of the polymers, which
can cause cell death and even organ failure. (Serpins are a superfamily of prot
eins with similar structures that were first recognized for their protease inhib
ition activity and are found in all kingdoms of life. Their unusual mechanism of
action irreversibly inhibits their target protease by undergoing a large confor
mational change to disrupt its active site. This contrasts with the more common
competitive mechanism for protease inhibitors that bind to and block access to t
he protease active site. Protease inhibition by serpins controls an array of bio
logical processes, including coagulation and inflammation, and consequently thes
e proteins are the target of medical research. Their conformational-change mecha
nism confers certain advantages, but it also has drawbacks: serpins are vulnerab
le to mutations that can result in protein misfolding and the formation of inact
ive long-chain polymers. Serpin polymerization not only reduces the amount of ac
tive inhibitor, but also leads to accumulation of the polymers, which can cause
cell death and even organ failure. (Serpins are a superfamily of proteins with s
imilar structures that were first recognized for their protease inhibition activ
ity and are found in all kingdoms of life. Their unusual mechanism of action irr
eversibly inhibits their target protease by undergoing a large conformational ch
ange to disrupt its active site. This contrasts with the more common competitive
mechanism for protease inhibitors that bind to and block access to the protease
active site. Protease inhibition by serpins controls an array of biological pro
cesses, including coagulation and inflammation, and consequently these proteins
are the target of medical research. Their conformational-change mechanism confer

s certain advantages, but it also has drawbacks: serpins are vulnerable to mutat
ions that can result in protein misfolding and the formation of inactive long-ch
ain polymers. Serpin polymerization not only reduces the amount of active inhibi
tor, but also leads to accumulation of the polymers, which can cause cell death
and even organ failure. (Serpins are a superfamily of proteins with similar stru
ctures that were first recognized for their protease inhibition activity and are
found in all kingdoms of life. Their unusual mechanism of action irreversibly i
nhibits their target protease by undergoing a large conformational change to dis
rupt its active site. This contrasts with the more common competitive mechanism
for protease inhibitors that bind to and block access to the protease active sit
e. Protease inhibition by serpins controls an array of biological processes, inc
luding coagulation and inflammation, and consequently these proteins are the tar
get of medical research. Their conformational-change mechanism confers certain a
dvantages, but it also has drawbacks: serpins are vulnerable to mutations that c
an result in protein misfolding and the formation of inactive long-chain polymer
s. Serpin polymerization not only reduces the amount of active inhibitor, but al
so leads to accumulation of the polymers, which can cause cell death and even or
gan failure. (Serpins are a superfamily of proteins with similar structures that
were first recognized for their protease inhibition activity and are found in a
ll kingdoms of life. Their unusual mechanism of action irreversibly inhibits the
ir target protease by undergoing a large conformational change to disrupt its ac
tive site. This contrasts with the more common competitive mechanism for proteas
e inhibitors that bind to and block access to the protease active site. Protease
inhibition by serpins controls an array of biological processes, including coag
ulation and inflammation, and consequently these proteins are the target of medi
cal research. Their conformational-change mechanism confers certain advantages,
but it also has drawbacks: serpins are vulnerable to mutations that can result i
n protein misfolding and the formation of inactive long-chain polymers. Serpin p
olymerization not only reduces the amount of active inhibitor, but also leads to
accumulation of the polymers, which can cause cell death and even organ failure
. (Serpins are a superfamily of proteins with similar structures that were first
recognized for their protease inhibition activity and are found in all kingdoms
of life. Their unusual mechanism of action irreversibly inhibits their target p
rotease by undergoing a large conformational change to disrupt its active site.
This contrasts with the more common competitive mechanism for protease inhibitor
s that bind to and block access to the protease active site. Protease inhibition
by serpins controls an array of biological processes, including coagulation and
inflammation, and consequently these proteins are the target of medical researc
h. Their conformational-change mechanism confers certain advantages, but it also
has drawbacks: serpins are vulnerable to mutations that can result in protein m
isfolding and the formation of inactive long-chain polymers. Serpin polymerizati
on not only reduces the amount of active inhibitor, but also leads to accumulati
on of the polymers, which can cause cell death and even organ failure. (Serpins
are a superfamily of proteins with similar structures that were first recognized
for their protease inhibition activity and are found in all kingdoms of life. T
heir unusual mechanism of action irreversibly inhibits their target protease by
undergoing a large conformational change to disrupt its active site. This contra
sts with the more common competitive mechanism for protease inhibitors that bind
to and block access to the protease active site. Protease inhibition by serpins
controls an array of biological processes, including coagulation and inflammati
on, and consequently these proteins are the target of medical research. Their co
nformational-change mechanism confers certain advantages, but it also has drawba
cks: serpins are vulnerable to mutations that can result in protein misfolding a
nd the formation of inactive long-chain polymers. Serpin polymerization not only
reduces the amount of active inhibitor, but also leads to accumulation of the p
olymers, which can cause cell death and even organ failure. (Serpins are a super
family of proteins with similar structures that were first recognized for their
protease inhibition activity and are found in all kingdoms of life. Their unusua
l mechanism of action irreversibly inhibits their target protease by undergoing
a large conformational change to disrupt its active site. This contrasts with th

e more common competitive mechanism for protease inhibitors that bind to and blo
ck access to the protease active site. Protease inhibition by serpins controls a
n array of biological processes, including coagulation and inflammation, and con
sequently these proteins are the target of medical research. Their conformationa
l-change mechanism confers certain advantages, but it also has drawbacks: serpin
s are vulnerable to mutations that can result in protein misfolding and the form
ation of inactive long-chain polymers. Serpin polymerization not only reduces th
e amount of active inhibitor, but also leads to accumulation of the polymers, wh
ich can cause cell death and even organ failure. (Serpins are a superfamily of p
roteins with similar structures that were first recognized for their protease in
hibition activity and are found in all kingdoms of life. Their unusual mechanism
of action irreversibly inhibits their target protease by undergoing a large con
formational change to disrupt its active site. This contrasts with the more comm
on competitive mechanism for protease inhibitors that bind to and block access t
o the protease active site. Protease inhibition by serpins controls an array of
biological processes, including coagulation and inflammation, and consequently t
hese proteins are the target of medical research. Their conformational-change me
chanism confers certain advantages, but it also has drawbacks: serpins are vulne
rable to mutations that can result in protein misfolding and the formation of in
active long-chain polymers. Serpin polymerization not only reduces the amount of
active inhibitor, but also leads to accumulation of the polymers, which can cau
se cell death and even organ failure. (Serpins are a superfamily of proteins wit
h similar structures that were first recognized for their protease inhibition ac
tivity and are found in all kingdoms of life. Their unusual mechanism of action
irreversibly inhibits their target protease by undergoing a large conformational
change to disrupt its active site. This contrasts with the more common competit
ive mechanism for protease inhibitors that bind to and block access to the prote
ase active site. Protease inhibition by serpins controls an array of biological
processes, including coagulation and inflammation, and consequently these protei
ns are the target of medical research. Their conformational-change mechanism con
fers certain advantages, but it also has drawbacks: serpins are vulnerable to mu
tations that can result in protein misfolding and the formation of inactive long
-chain polymers. Serpin polymerization not only reduces the amount of active inh
ibitor, but also leads to accumulation of the polymers, which can cause cell dea
th and even organ failure. (Serpins are a superfamily of proteins with similar s
tructures that were first recognized for their protease inhibition activity and
are found in all kingdoms of life. Their unusual mechanism of action irreversibl
y inhibits their target protease by undergoing a large conformational change to
disrupt its active site. This contrasts with the more common competitive mechani
sm for protease inhibitors that bind to and block access to the protease active
site. Protease inhibition by serpins controls an array of biological processes,
including coagulation and inflammation, and consequently these proteins are the
target of medical research. Their conformational-change mechanism confers certai
n advantages, but it also has drawbacks: serpins are vulnerable to mutations tha
t can result in protein misfolding and the formation of inactive long-chain poly
mers. Serpin polymerization not only reduces the amount of active inhibitor, but
also leads to accumulation of the polymers, which can cause cell death and even
organ failure. (Serpins are a superfamily of proteins with similar structures t
hat were first recognized for their protease inhibition activity and are found i
n all kingdoms of life. Their unusual mechanism of action irreversibly inhibits
their target protease by undergoing a large conformational change to disrupt its
active site. This contrasts with the more common competitive mechanism for prot
ease inhibitors that bind to and block access to the protease active site. Prote
ase inhibition by serpins controls an array of biological processes, including c
oagulation and inflammation, and consequently these proteins are the target of m
edical research. Their conformational-change mechanism confers certain advantage
s, but it also has drawbacks: serpins are vulnerable to mutations that can resul
t in protein misfolding and the formation of inactive long-chain polymers. Serpi
n polymerization not only reduces the amount of active inhibitor, but also leads
to accumulation of the polymers, which can cause cell death and even organ fail

ure. (Serpins are a superfamily of proteins with similar structures that were fi
rst recognized for their protease inhibition activity and are found in all kingd
oms of life. Their unusual mechanism of action irreversibly inhibits their targe
t protease by undergoing a large conformational change to disrupt its active sit
e. This contrasts with the more common competitive mechanism for protease inhibi
tors that bind to and block access to the protease active site. Protease inhibit
ion by serpins controls an array of biological processes, including coagulation
and inflammation, and consequently these proteins are the target of medical rese
arch. Their conformational-change mechanism confers certain advantages, but it a
lso has drawbacks: serpins are vulnerable to mutations that can result in protei
n misfolding and the formation of inactive long-chain polymers. Serpin polymeriz
ation not only reduces the amount of active inhibitor, but also leads to accumul
ation of the polymers, which can cause cell death and even organ failure. (Serpi
ns are a superfamily of proteins with similar structures that were first recogni
zed for their protease inhibition activity and are found in all kingdoms of life
. Their unusual mechanism of action irreversibly inhibits their target protease
by undergoing a large conformational change to disrupt its active site. This con
trasts with the more common competitive mechanism for protease inhibitors that b
ind to and block access to the protease active site. Protease inhibition by serp
ins controls an array of biological processes, including coagulation and inflamm
ation, and consequently these proteins are the target of medical research. Their
conformational-change mechanism confers certain advantages, but it also has dra
wbacks: serpins are vulnerable to mutations that can result in protein misfoldin
g and the formation of inactive long-chain polymers. Serpin polymerization not o
nly reduces the amount of active inhibitor, but also leads to accumulation of th
e polymers, which can cause cell death and even organ failure. (Serpins are a su
perfamily of proteins with similar structures that were first recognized for the
ir protease inhibition activity and are found in all kingdoms of life. Their unu
sual mechanism of action irreversibly inhibits their target protease by undergoi
ng a large conformational change to disrupt its active site. This contrasts with
the more common competitive mechanism for protease inhibitors that bind to and
block access to the protease active site. Protease inhibition by serpins control
s an array of biological processes, including coagulation and inflammation, and
consequently these proteins are the target of medical research. Their conformati
onal-change mechanism confers certain advantages, but it also has drawbacks: ser
pins are vulnerable to mutations that can result in protein misfolding and the f
ormation of inactive long-chain polymers. Serpin polymerization not only reduces
the amount of active inhibitor, but also leads to accumulation of the polymers,
which can cause cell death and even organ failure. (Serpins are a superfamily o
f proteins with similar structures that were first recognized for their protease
inhibition activity and are found in all kingdoms of life. Their unusual mechan
ism of action irreversibly inhibits their target protease by undergoing a large
conformational change to disrupt its active site. This contrasts with the more c
ommon competitive mechanism for protease inhibitors that bind to and block acces
s to the protease active site. Protease inhibition by serpins controls an array
of biological processes, including coagulation and inflammation, and consequentl
y these proteins are the target of medical research. Their conformational-change
mechanism confers certain advantages, but it also has drawbacks: serpins are vu
lnerable to mutations that can result in protein misfolding and the formation of
inactive long-chain polymers. Serpin polymerization not only reduces the amount
of active inhibitor, but also leads to accumulation of the polymers, which can
cause cell death and even organ failure. (Serpins are a superfamily of proteins
with similar structures that were first recognized for their protease inhibition
activity and are found in all kingdoms of life. Their unusual mechanism of acti
on irreversibly inhibits their target protease by undergoing a large conformatio
nal change to disrupt its active site. This contrasts with the more common compe
titive mechanism for protease inhibitors that bind to and block access to the pr
otease active site. Protease inhibition by serpins controls an array of biologic
al processes, including coagulation and inflammation, and consequently these pro
teins are the target of medical research. Their conformational-change mechanism

confers certain advantages, but it also has drawbacks: serpins are vulnerable to
mutations that can result in protein misfolding and the formation of inactive l
ong-chain polymers. Serpin polymerization not only reduces the amount of active
inhibitor, but also leads to accumulation of the polymers, which can cause cell
death and even organ failure. (Serpins are a superfamily of proteins with simila
r structures that were first recognized for their protease inhibition activity a
nd are found in all kingdoms of life. Their unusual mechanism of action irrevers
ibly inhibits their target protease by undergoing a large conformational change
to disrupt its active site. This contrasts with the more common competitive mech
anism for protease inhibitors that bind to and block access to the protease acti
ve site. Protease inhibition by serpins controls an array of biological processe
s, including coagulation and inflammation, and consequently these proteins are t
he target of medical research. Their conformational-change mechanism confers cer
tain advantages, but it also has drawbacks: serpins are vulnerable to mutations
that can result in protein misfolding and the formation of inactive long-chain p
olymers. Serpin polymerization not only reduces the amount of active inhibitor,
but also leads to accumulation of the polymers, which can cause cell death and e
ven organ failure. (Serpins are a superfamily of proteins with similar structure
s that were first recognized for their protease inhibition activity and are foun
d in all kingdoms of life. Their unusual mechanism of action irreversibly inhibi
ts their target protease by undergoing a large conformational change to disrupt
its active site. This contrasts with the more common competitive mechanism for p
rotease inhibitors that bind to and block access to the protease active site. Pr
otease inhibition by serpins controls an array of biological processes, includin
g coagulation and inflammation, and consequently these proteins are the target o
f medical research. Their conformational-change mechanism confers certain advant
ages, but it also has drawbacks: serpins are vulnerable to mutations that can re
sult in protein misfolding and the formation of inactive long-chain polymers. Se
rpin polymerization not only reduces the amount of active inhibitor, but also le
ads to accumulation of the polymers, which can cause cell death and even organ f
ailure. (Serpins are a superfamily of proteins with similar structures that were
first recognized for their protease inhibition activity and are found in all ki
ngdoms of life. Their unusual mechanism of action irreversibly inhibits their ta
rget protease by undergoing a large conformational change to disrupt its active
site. This contrasts with the more common competitive mechanism for protease inh
ibitors that bind to and block access to the protease active site. Protease inhi
bition by serpins controls an array of biological processes, including coagulati
on and inflammation, and consequently these proteins are the target of medical r
esearch. Their conformational-change mechanism confers certain advantages, but i
t also has drawbacks: serpins are vulnerable to mutations that can result in pro
tein misfolding and the formation of inactive long-chain polymers. Serpin polyme
rization not only reduces the amount of active inhibitor, but also leads to accu
mulation of the polymers, which can cause cell death and even organ failure. (Se
rpins are a superfamily of proteins with similar structures that were first reco
gnized for their protease inhibition activity and are found in all kingdoms of l
ife. Their unusual mechanism of action irreversibly inhibits their target protea
se by undergoing a large conformational change to disrupt its active site. This
contrasts with the more common competitive mechanism for protease inhibitors tha
t bind to and block access to the protease active site. Protease inhibition by s
erpins controls an array of biological processes, including coagulation and infl
ammation, and consequently these proteins are the target of medical research. Th
eir conformational-change mechanism confers certain advantages, but it also has
drawbacks: serpins are vulnerable to mutations that can result in protein misfol
ding and the formation of inactive long-chain polymers. Serpin polymerization no
t only reduces the amount of active inhibitor, but also leads to accumulation of
the polymers, which can cause cell death and even organ failure. (Serpins are a
superfamily of proteins with similar structures that were first recognized for
their protease inhibition activity and are found in all kingdoms of life. Their
unusual mechanism of action irreversibly inhibits their target protease by under
going a large conformational change to disrupt its active site. This contrasts w

ith the more common competitive mechanism for protease inhibitors that bind to a
nd block access to the protease active site. Protease inhibition by serpins cont
rols an array of biological processes, including coagulation and inflammation, a
nd consequently these proteins are the target of medical research. Their conform
ational-change mechanism confers certain advantages, but it also has drawbacks:
serpins are vulnerable to mutations that can result in protein misfolding and th
e formation of inactive long-chain polymers. Serpin polymerization not only redu
ces the amount of active inhibitor, but also leads to accumulation of the polyme
rs, which can cause cell death and even organ failure. (Serpins are a superfamil
y of proteins with similar structures that were first recognized for their prote
ase inhibition activity and are found in all kingdoms of life. Their unusual mec
hanism of action irreversibly inhibits their target protease by undergoing a lar
ge conformational change to disrupt its active site. This contrasts with the mor
e common competitive mechanism for protease inhibitors that bind to and block ac
cess to the protease active site. Protease inhibition by serpins controls an arr
ay of biological processes, including coagulation and inflammation, and conseque
ntly these proteins are the target of medical research. Their conformational-cha
nge mechanism confers certain advantages, but it also has drawbacks: serpins are
vulnerable to mutations that can result in protein misfolding and the formation
of inactive long-chain polymers. Serpin polymerization not only reduces the amo
unt of active inhibitor, but also leads to accumulation of the polymers, which c
an cause cell death and even organ failure. (Serpins are a superfamily of protei
ns with similar structures that were first recognized for their protease inhibit
ion activity and are found in all kingdoms of life. Their unusual mechanism of a
ction irreversibly inhibits their target protease by undergoing a large conforma
tional change to disrupt its active site. This contrasts with the more common co
mpetitive mechanism for protease inhibitors that bind to and block access to the
protease active site. Protease inhibition by serpins controls an array of biolo
gical processes, including coagulation and inflammation, and consequently these
proteins are the target of medical research. Their conformational-change mechani
sm confers certain advantages, but it also has drawbacks: serpins are vulnerable
to mutations that can result in protein misfolding and the formation of inactiv
e long-chain polymers. Serpin polymerization not only reduces the amount of acti
ve inhibitor, but also leads to accumulation of the polymers, which can cause ce
ll death and even organ failure. (Serpins are a superfamily of proteins with sim
ilar structures that were first recognized for their protease inhibition activit
y and are found in all kingdoms of life. Their unusual mechanism of action irrev
ersibly inhibits their target protease by undergoing a large conformational chan
ge to disrupt its active site. This contrasts with the more common competitive m
echanism for protease inhibitors that bind to and block access to the protease a
ctive site. Protease inhibition by serpins controls an array of biological proce
sses, including coagulation and inflammation, and consequently these proteins ar
e the target of medical research. Their conformational-change mechanism confers
certain advantages, but it also has drawbacks: serpins are vulnerable to mutatio
ns that can result in protein misfolding and the formation of inactive long-chai
n polymers. Serpin polymerization not only reduces the amount of active inhibito
r, but also leads to accumulation of the polymers, which can cause cell death an
d even organ failure. (Serpins are a superfamily of proteins with similar struct
ures that were first recognized for their protease inhibition activity and are f
ound in all kingdoms of life. Their unusual mechanism of action irreversibly inh
ibits their target protease by undergoing a large conformational change to disru
pt its active site. This contrasts with the more common competitive mechanism fo
r protease inhibitors that bind to and block access to the protease active site.
Protease inhibition by serpins controls an array of biological processes, inclu
ding coagulation and inflammation, and consequently these proteins are the targe
t of medical research. Their conformational-change mechanism confers certain adv
antages, but it also has drawbacks: serpins are vulnerable to mutations that can
result in protein misfolding and the formation of inactive long-chain polymers.
Serpin polymerization not only reduces the amount of active inhibitor, but also
leads to accumulation of the polymers, which can cause cell death and even orga

n failure. (Serpins are a superfamily of proteins with similar structures that w

ere first recognized for their protease inhibition activity and are found in all
kingdoms of life. Their unusual mechanism of action irreversibly inhibits their
target protease by undergoing a large conformational change to disrupt its acti
ve site. This contrasts with the more common competitive mechanism for protease
inhibitors that bind to and block access to the protease active site. Protease i
nhibition by serpins controls an array of biological processes, including coagul
ation and inflammation, and consequently these proteins are the target of medica
l research. Their conformational-change mechanism confers certain advantages, bu
t it also has drawbacks: serpins are vulnerable to mutations that can result in
protein misfolding and the formation of inactive long-chain polymers. Serpin pol
ymerization not only reduces the amount of active inhibitor, but also leads to a
ccumulation of the polymers, which can cause cell death and even organ failure.
(Serpins are a superfamily of proteins with similar structures that were first r
ecognized for their protease inhibition activity and are found in all kingdoms o
f life. Their unusual mechanism of action irreversibly inhibits their target pro
tease by undergoing a large conformational change to disrupt its active site. Th
is contrasts with the more common competitive mechanism for protease inhibitors
that bind to and block access to the protease active site. Protease inhibition b
y serpins controls an array of biological processes, including coagulation and i
nflammation, and consequently these proteins are the target of medical research.
Their conformational-change mechanism confers certain advantages, but it also h
as drawbacks: serpins are vulnerable to mutations that can result in protein mis
folding and the formation of inactive long-chain polymers. Serpin polymerization
not only reduces the amount of active inhibitor, but also leads to accumulation
of the polymers, which can cause cell death and even organ failure. (Serpins ar
e a superfamily of proteins with similar structures that were first recognized f
or their protease inhibition activity and are found in all kingdoms of life. The
ir unusual mechanism of action irreversibly inhibits their target protease by un
dergoing a large conformational change to disrupt its active site. This contrast
s with the more common competitive mechanism for protease inhibitors that bind t
o and block access to the protease active site. Protease inhibition by serpins c
ontrols an array of biological processes, including coagulation and inflammation
, and consequently these proteins are the target of medical research. Their conf
ormational-change mechanism confers certain advantages, but it also has drawback
s: serpins are vulnerable to mutations that can result in protein misfolding and
the formation of inactive long-chain polymers. Serpin polymerization not only r
educes the amount of active inhibitor, but also leads to accumulation of the pol
ymers, which can cause cell death and even organ failure. (Serpins are a superfa
mily of proteins with similar structures that were first recognized for their pr
otease inhibition activity and are found in all kingdoms of life. Their unusual
mechanism of action irreversibly inhibits their target protease by undergoing a
large conformational change to disrupt its active site. This contrasts with the
more common competitive mechanism for protease inhibitors that bind to and block
access to the protease active site. Protease inhibition by serpins controls an
array of biological processes, including coagulation and inflammation, and conse
quently these proteins are the target of medical research. Their conformationalchange mechanism confers certain advantages, but it also has drawbacks: serpins
are vulnerable to mutations that can result in protein misfolding and the format
ion of inactive long-chain polymers. Serpin polymerization not only reduces the
amount of active inhibitor, but also leads to accumulation of the polymers, whic
h can cause cell death and even organ failure. (Serpins are a superfamily of pro
teins with similar structures that were first recognized for their protease inhi
bition activity and are found in all kingdoms of life. Their unusual mechanism o
f action irreversibly inhibits their target protease by undergoing a large confo
rmational change to disrupt its active site. This contrasts with the more common
competitive mechanism for protease inhibitors that bind to and block access to
the protease active site. Protease inhibition by serpins controls an array of bi
ological processes, including coagulation and inflammation, and consequently the
se proteins are the target of medical research. Their conformational-change mech

anism confers certain advantages, but it also has drawbacks: serpins are vulnera
ble to mutations that can result in protein misfolding and the formation of inac
tive long-chain polymers. Serpin polymerization not only reduces the amount of a
ctive inhibitor, but also leads to accumulation of the polymers, which can cause
cell death and even organ failure. (Serpins are a superfamily of proteins with
similar structures that were first recognized for their protease inhibition acti
vity and are found in all kingdoms of life. Their unusual mechanism of action ir
reversibly inhibits their target protease by undergoing a large conformational c
hange to disrupt its active site. This contrasts with the more common competitiv
e mechanism for protease inhibitors that bind to and block access to the proteas
e active site. Protease inhibition by serpins controls an array of biological pr
ocesses, including coagulation and inflammation, and consequently these proteins
are the target of medical research. Their conformational-change mechanism confe
rs certain advantages, but it also has drawbacks: serpins are vulnerable to muta
tions that can result in protein misfolding and the formation of inactive long-c
hain polymers. Serpin polymerization not only reduces the amount of active inhib
itor, but also leads to accumulation of the polymers, which can cause cell death
and even organ failure. (Serpins are a superfamily of proteins with similar str
uctures that were first recognized for their protease inhibition activity and ar
e found in all kingdoms of life. Their unusual mechanism of action irreversibly
inhibits their target protease by undergoing a large conformational change to di
srupt its active site. This contrasts with the more common competitive mechanism
for protease inhibitors that bind to and block access to the protease active si
te. Protease inhibition by serpins controls an array of biological processes, in
cluding coagulation and inflammation, and consequently these proteins are the ta
rget of medical research. Their conformational-change mechanism confers certain
advantages, but it also has drawbacks: serpins are vulnerable to mutations that
can result in protein misfolding and the formation of inactive long-chain polyme
rs. Serpin polymerization not only reduces the amount of active inhibitor, but a
lso leads to accumulation of the polymers, which can cause cell death and even o
rgan failure. (Serpins are a superfamily of proteins with similar structures tha
t were first recognized for their protease inhibition activity and are found in
all kingdoms of life. Their unusual mechanism of action irreversibly inhibits th
eir target protease by undergoing a large conformational change to disrupt its a
ctive site. This contrasts with the more common competitive mechanism for protea
se inhibitors that bind to and block access to the protease active site. Proteas
e inhibition by serpins controls an array of biological processes, including coa
gulation and inflammation, and consequently these proteins are the target of med
ical research. Their conformational-change mechanism confers certain advantages,
but it also has drawbacks: serpins are vulnerable to mutations that can result
in protein misfolding and the formation of inactive long-chain polymers. Serpin
polymerization not only reduces the amount of active inhibitor, but also leads t
o accumulation of the polymers, which can cause cell death and even organ failur
e. (Serpins are a superfamily of proteins with similar structures that were firs
t recognized for their protease inhibition activity and are found in all kingdom
s of life. Their unusual mechanism of action irreversibly inhibits their target
protease by undergoing a large conformational change to disrupt its active site.
This contrasts with the more common competitive mechanism for protease inhibito
rs that bind to and block access to the protease active site. Protease inhibitio
n by serpins controls an array of biological processes, including coagulation an
d inflammation, and consequently these proteins are the target of medical resear
ch. Their conformational-change mechanism confers certain advantages, but it als
o has drawbacks: serpins are vulnerable to mutations that can result in protein
misfolding and the formation of inactive long-chain polymers. Serpin polymerizat
ion not only reduces the amount of active inhibitor, but also leads to accumulat
ion of the polymers, which can cause cell death and even organ failure. (Serpins
are a superfamily of proteins with similar structures that were first recognize
d for their protease inhibition activity and are found in all kingdoms of life.
Their unusual mechanism of action irreversibly inhibits their target protease by
undergoing a large conformational change to disrupt its active site. This contr

asts with the more common competitive mechanism for protease inhibitors that bin
d to and block access to the protease active site. Protease inhibition by serpin
s controls an array of biological processes, including coagulation and inflammat
ion, and consequently these proteins are the target of medical research. Their c
onformational-change mechanism confers certain advantages, but it also has drawb
acks: serpins are vulnerable to mutations that can result in protein misfolding
and the formation of inactive long-chain polymers. Serpin polymerization not onl
y reduces the amount of active inhibitor, but also leads to accumulation of the
polymers, which can cause cell death and even organ failure. (Serpins are a supe
rfamily of proteins with similar structures that were first recognized for their
protease inhibition activity and are found in all kingdoms of life. Their unusu
al mechanism of action irreversibly inhibits their target protease by undergoing
a large conformational change to disrupt its active site. This contrasts with t
he more common competitive mechanism for protease inhibitors that bind to and bl
ock access to the protease active site. Protease inhibition by serpins controls
an array of biological processes, including coagulation and inflammation, and co
nsequently these proteins are the target of medical research. Their conformation
al-change mechanism confers certain advantages, but it also has drawbacks: serpi
ns are vulnerable to mutations that can result in protein misfolding and the for
mation of inactive long-chain polymers. Serpin polymerization not only reduces t
he amount of active inhibitor, but also leads to accumulation of the polymers, w
hich can cause cell death and even organ failure. (Serpins are a superfamily of
proteins with similar structures that were first recognized for their protease i
nhibition activity and are found in all kingdoms of life. Their unusual mechanis
m of action irreversibly inhibits their target protease by undergoing a large co
nformational change to disrupt its active site. This contrasts with the more com
mon competitive mechanism for protease inhibitors that bind to and block access
to the protease active site. Protease inhibition by serpins controls an array of
biological processes, including coagulation and inflammation, and consequently
these proteins are the target of medical research. Their conformational-change m
echanism confers certain advantages, but it also has drawbacks: serpins are vuln
erable to mutations that can result in protein misfolding and the formation of i
nactive long-chain polymers. Serpin polymerization not only reduces the amount o
f active inhibitor, but also leads to accumulation of the polymers, which can ca
use cell death and even organ failure. (Serpins are a superfamily of proteins wi
th similar structures that were first recognized for their protease inhibition a
ctivity and are found in all kingdoms of life. Their unusual mechanism of action
irreversibly inhibits their target protease by undergoing a large conformationa
l change to disrupt its active site. This contrasts with the more common competi
tive mechanism for protease inhibitors that bind to and block access to the prot
ease active site. Protease inhibition by serpins controls an array of biological
processes, including coagulation and inflammation, and consequently these prote
ins are the target of medical research. Their conformational-change mechanism co
nfers certain advantages, but it also has drawbacks: serpins are vulnerable to m
utations that can result in protein misfolding and the formation of inactive lon
g-chain polymers. Serpin polymerization not only reduces the amount of active in
hibitor, but also leads to accumulation of the polymers, which can cause cell de
ath and even organ failure. (Serpins are a superfamily of proteins with similar
structures that were first recognized for their protease inhibition activity and
are found in all kingdoms of life. Their unusual mechanism of action irreversib
ly inhibits their target protease by undergoing a large conformational change to
disrupt its active site. This contrasts with the more common competitive mechan
ism for protease inhibitors that bind to and block access to the protease active
site. Protease inhibition by serpins controls an array of biological processes,
including coagulation and inflammation, and consequently these proteins are the
target of medical research. Their conformational-change mechanism confers certa
in advantages, but it also has drawbacks: serpins are vulnerable to mutations th
at can result in protein misfolding and the formation of inactive long-chain pol
ymers. Serpin polymerization not only reduces the amount of active inhibitor, bu
t also leads to accumulation of the polymers, which can cause cell death and eve

n organ failure. (Serpins are a superfamily of proteins with similar structures

that were first recognized for their protease inhibition activity and are found
in all kingdoms of life. Their unusual mechanism of action irreversibly inhibits
their target protease by undergoing a large conformational change to disrupt it
s active site. This contrasts with the more common competitive mechanism for pro
tease inhibitors that bind to and block access to the protease active site. Prot
ease inhibition by serpins controls an array of biological processes, including
coagulation and inflammation, and consequently these proteins are the target of
medical research. Their conformational-change mechanism confers certain advantag
es, but it also has drawbacks: serpins are vulnerable to mutations that can resu
lt in protein misfolding and the formation of inactive long-chain polymers. Serp
in polymerization not only reduces the amount of active inhibitor, but also lead
s to accumulation of the polymers, which can cause cell death and even organ fai
lure. (Serpins are a superfamily of proteins with similar structures that were f
irst recognized for their protease inhibition activity and are found in all king
doms of life. Their unusual mechanism of action irreversibly inhibits their targ
et protease by undergoing a large conformational change to disrupt its active si
te. This contrasts with the more common competitive mechanism for protease inhib
itors that bind to and block access to the protease active site. Protease inhibi
tion by serpins controls an array of biological processes, including coagulation
and inflammation, and consequently these proteins are the target of medical res
earch. Their conformational-change mechanism confers certain advantages, but it
also has drawbacks: serpins are vulnerable to mutations that can result in prote
in misfolding and the formation of inactive long-chain polymers. Serpin polymeri
zation not only reduces the amount of active inhibitor, but also leads to accumu
lation of the polymers, which can cause cell death and even organ failure. (Serp
ins are a superfamily of proteins with similar structures that were first recogn
ized for their protease inhibition activity and are found in all kingdoms of lif
e. Their unusual mechanism of action irreversibly inhibits their target protease
by undergoing a large conformational change to disrupt its active site. This co
ntrasts with the more common competitive mechanism for protease inhibitors that
bind to and block access to the protease active site. Protease inhibition by ser
pins controls an array of biological processes, including coagulation and inflam
mation, and consequently these proteins are the target of medical research. Thei
r conformational-change mechanism confers certain advantages, but it also has dr
awbacks: serpins are vulnerable to mutations that can result in protein misfoldi
ng and the formation of inactive long-chain polymers. Serpin polymerization not
only reduces the amount of active inhibitor, but also leads to accumulation of t
he polymers, which can cause cell death and even organ failure. (Serpins are a s
uperfamily of proteins with similar structures that were first recognized for th
eir protease inhibition activity and are found in all kingdoms of life. Their un
usual mechanism of action irreversibly inhibits their target protease by undergo
ing a large conformational change to disrupt its active site. This contrasts wit
h the more common competitive mechanism for protease inhibitors that bind to and
block access to the protease active site. Protease inhibition by serpins contro
ls an array of biological processes, including coagulation and inflammation, and
consequently these proteins are the target of medical research. Their conformat
ional-change mechanism confers certain advantages, but it also has drawbacks: se
rpins are vulnerable to mutations that can result in protein misfolding and the
formation of inactive long-chain polymers. Serpin polymerization not only reduce
s the amount of active inhibitor, but also leads to accumulation of the polymers
, which can cause cell death and even organ failure. (Serpins are a superfamily
of proteins with similar structures that were first recognized for their proteas
e inhibition activity and are found in all kingdoms of life. Their unusual mecha
nism of action irreversibly inhibits their target protease by undergoing a large
conformational change to disrupt its active site. This contrasts with the more
common competitive mechanism for protease inhibitors that bind to and block acce
ss to the protease active site. Protease inhibition by serpins controls an array
of biological processes, including coagulation and inflammation, and consequent
ly these proteins are the target of medical research. Their conformational-chang

e mechanism confers certain advantages, but it also has drawbacks: serpins are v
ulnerable to mutations that can result in protein misfolding and the formation o
f inactive long-chain polymers. Serpin polymerization not only reduces the amoun
t of active inhibitor, but also leads to accumulation of the polymers, which can
cause cell death and even organ failure. (Serpins are a superfamily of proteins
with similar structures that were first recognized for their protease inhibitio
n activity and are found in all kingdoms of life. Their unusual mechanism of act
ion irreversibly inhibits their target protease by undergoing a large conformati
onal change to disrupt its active site. This contrasts with the more common comp
etitive mechanism for protease inhibitors that bind to and block access to the p
rotease active site. Protease inhibition by serpins controls an array of biologi
cal processes, including coagulation and inflammation, and consequently these pr
oteins are the target of medical research. Their conformational-change mechanism
confers certain advantages, but it also has drawbacks: serpins are vulnerable t
o mutations that can result in protein misfolding and the formation of inactive
long-chain polymers. Serpin polymerization not only reduces the amount of active
inhibitor, but also leads to accumulation of the polymers, which can cause cell
death and even organ failure. (Serpins are a superfamily of proteins with simil
ar structures that were first recognized for their protease inhibition activity
and are found in all kingdoms of life. Their unusual mechanism of action irrever
sibly inhibits their target protease by undergoing a large conformational change
to disrupt its active site. This contrasts with the more common competitive mec
hanism for protease inhibitors that bind to and block access to the protease act
ive site. Protease inhibition by serpins controls an array of biological process
es, including coagulation and inflammation, and consequently these proteins are
the target of medical research. Their conformational-change mechanism confers ce
rtain advantages, but it also has drawbacks: serpins are vulnerable to mutations
that can result in protein misfolding and the formation of inactive long-chain
polymers. Serpin polymerization not only reduces the amount of active inhibitor,
but also leads to accumulation of the polymers, which can cause cell death and
even organ failure. (Serpins are a superfamily of proteins with similar structur
es that were first recognized for their protease inhibition activity and are fou
nd in all kingdoms of life. Their unusual mechanism of action irreversibly inhib
its their target protease by undergoing a large conformational change to disrupt
its active site. This contrasts with the more common competitive mechanism for
protease inhibitors that bind to and block access to the protease active site. P
rotease inhibition by serpins controls an array of biological processes, includi
ng coagulation and inflammation, and consequently these proteins are the target
of medical research. Their conformational-change mechanism confers certain advan
tages, but it also has drawbacks: serpins are vulnerable to mutations that can r
esult in protein misfolding and the formation of inactive long-chain polymers. S
erpin polymerization not only reduces the amount of active inhibitor, but also l
eads to accumulation of the polymers, which can cause cell death and even organ
failure. (Serpins are a superfamily of proteins with similar structures that wer
e first recognized for their protease inhibition activity and are found in all k
ingdoms of life. Their unusual mechanism of action irreversibly inhibits their t
arget protease by undergoing a large conformational change to disrupt its active
site. This contrasts with the more common competitive mechanism for protease in
hibitors that bind to and block access to the protease active site. Protease inh
ibition by serpins controls an array of biological processes, including coagulat
ion and inflammation, and consequently these proteins are the target of medical
research. Their conformational-change mechanism confers certain advantages, but
it also has drawbacks: serpins are vulnerable to mutations that can result in pr
otein misfolding and the formation of inactive long-chain polymers. Serpin polym
erization not only reduces the amount of active inhibitor, but also leads to acc
umulation of the polymers, which can cause cell death and even organ failure. (S
erpins are a superfamily of proteins with similar structures that were first rec
ognized for their protease inhibition activity and are found in all kingdoms of
life. Their unusual mechanism of action irreversibly inhibits their target prote
ase by undergoing a large conformational change to disrupt its active site. This

contrasts with the more common competitive mechanism for protease inhibitors th
at bind to and block access to the protease active site. Protease inhibition by
serpins controls an array of biological processes, including coagulation and inf
lammation, and consequently these proteins are the target of medical research. T
heir conformational-change mechanism confers certain advantages, but it also has
drawbacks: serpins are vulnerable to mutations that can result in protein misfo
lding and the formation of inactive long-chain polymers. Serpin polymerization n
ot only reduces the amount of active inhibitor, but also leads to accumulation o
f the polymers, which can cause cell death and even organ failure. (Serpins are
a superfamily of proteins with similar structures that were first recognized for
their protease inhibition activity and are found in all kingdoms of life. Their
unusual mechanism of action irreversibly inhibits their target protease by unde
rgoing a large conformational change to disrupt its active site. This contrasts
with the more common competitive mechanism for protease inhibitors that bind to
and block access to the protease active site. Protease inhibition by serpins con
trols an array of biological processes, including coagulation and inflammation,
and consequently these proteins are the target of medical research. Their confor
mational-change mechanism confers certain advantages, but it also has drawbacks:
serpins are vulnerable to mutations that can result in protein misfolding and t
he formation of inactive long-chain polymers. Serpin polymerization not only red
uces the amount of active inhibitor, but also leads to accumulation of the polym
ers, which can cause cell death and even organ failure. (Serpins are a superfami
ly of proteins with similar structures that were first recognized for their prot
ease inhibition activity and are found in all kingdoms of life. Their unusual me
chanism of action irreversibly inhibits their target protease by undergoing a la
rge conformational change to disrupt its active site. This contrasts with the mo
re common competitive mechanism for protease inhibitors that bind to and block a
ccess to the protease active site. Protease inhibition by serpins controls an ar
ray of biological processes, including coagulation and inflammation, and consequ
ently these proteins are the target of medical research. Their conformational-ch
ange mechanism confers certain advantages, but it also has drawbacks: serpins ar
e vulnerable to mutations that can result in protein misfolding and the formatio
n of inactive long-chain polymers. Serpin polymerization not only reduces the am
ount of active inhibitor, but also leads to accumulation of the polymers, which
can cause cell death and even organ failure. (Serpins are a superfamily of prote
ins with similar structures that were first recognized for their protease inhibi
tion activity and are found in all kingdoms of life. Their unusual mechanism of
action irreversibly inhibits their target protease by undergoing a large conform
ational change to disrupt its active site. This contrasts with the more common c
ompetitive mechanism for protease inhibitors that bind to and block access to th
e protease active site. Protease inhibition by serpins controls an array of biol
ogical processes, including coagulation and inflammation, and consequently these
proteins are the target of medical research. Their conformational-change mechan
ism confers certain advantages, but it also has drawbacks: serpins are vulnerabl
e to mutations that can result in protein misfolding and the formation of inacti
ve long-chain polymers. Serpin polymerization not only reduces the amount of act
ive inhibitor, but also leads to accumulation of the polymers, which can cause c
ell death and even organ failure. (Serpins are a superfamily of proteins with si
milar structures that were first recognized for their protease inhibition activi
ty and are found in all kingdoms of life. Their unusual mechanism of action irre
versibly inhibits their target protease by undergoing a large conformational cha
nge to disrupt its active site. This contrasts with the more common competitive
mechanism for protease inhibitors that bind to and block access to the protease
active site. Protease inhibition by serpins controls an array of biological proc
esses, including coagulation and inflammation, and consequently these proteins a
re the target of medical research. Their conformational-change mechanism confers
certain advantages, but it also has drawbacks: serpins are vulnerable to mutati
ons that can result in protein misfolding and the formation of inactive long-cha
in polymers. Serpin polymerization not only reduces the amount of active inhibit
or, but also leads to accumulation of the polymers, which can cause cell death a

nd even organ failure. (Serpins are a superfamily of proteins with similar struc
tures that were first recognized for their protease inhibition activity and are
found in all kingdoms of life. Their unusual mechanism of action irreversibly in
hibits their target protease by undergoing a large conformational change to disr
upt its active site. This contrasts with the more common competitive mechanism f
or protease inhibitors that bind to and block access to the protease active site
. Protease inhibition by serpins controls an array of biological processes, incl
uding coagulation and inflammation, and consequently these proteins are the targ
et of medical research. Their conformational-change mechanism confers certain ad
vantages, but it also has drawbacks: serpins are vulnerable to mutations that ca
n result in protein misfolding and the formation of inactive long-chain polymers
. Serpin polymerization not only reduces the amount of active inhibitor, but als
o leads to accumulation of the polymers, which can cause cell death and even org
an failure. (Serpins are a superfamily of proteins with similar structures that
were first recognized for their protease inhibition activity and are found in al
l kingdoms of life. Their unusual mechanism of action irreversibly inhibits thei
r target protease by undergoing a large conformational change to disrupt its act
ive site. This contrasts with the more common competitive mechanism for protease
inhibitors that bind to and block access to the protease active site. Protease
inhibition by serpins controls an array of biological processes, including coagu
lation and inflammation, and consequently these proteins are the target of medic
al research. Their conformational-change mechanism confers certain advantages, b
ut it also has drawbacks: serpins are vulnerable to mutations that can result in
protein misfolding and the formation of inactive long-chain polymers. Serpin po
lymerization not only reduces the amount of active inhibitor, but also leads to
accumulation of the polymers, which can cause cell death and even organ failure.
(Serpins are a superfamily of proteins with similar structures that were first
recognized for their protease inhibition activity and are found in all kingdoms
of life. Their unusual mechanism of action irreversibly inhibits their target pr
otease by undergoing a large conformational change to disrupt its active site. T
his contrasts with the more common competitive mechanism for protease inhibitors
that bind to and block access to the protease active site. Protease inhibition
by serpins controls an array of biological processes, including coagulation and
inflammation, and consequently these proteins are the target of medical research
. Their conformational-change mechanism confers certain advantages, but it also
has drawbacks: serpins are vulnerable to mutations that can result in protein mi
sfolding and the formation of inactive long-chain polymers. Serpin polymerizatio
n not only reduces the amount of active inhibitor, but also leads to accumulatio
n of the polymers, which can cause cell death and even organ failure. (Serpins a
re a superfamily of proteins with similar structures that were first recognized
for their protease inhibition activity and are found in all kingdoms of life. Th
eir unusual mechanism of action irreversibly inhibits their target protease by u
ndergoing a large conformational change to disrupt its active site. This contras
ts with the more common competitive mechanism for protease inhibitors that bind
to and block access to the protease active site. Protease inhibition by serpins
controls an array of biological processes, including coagulation and inflammatio
n, and consequently these proteins are the target of medical research. Their con
formational-change mechanism confers certain advantages, but it also has drawbac
ks: serpins are vulnerable to mutations that can result in protein misfolding an
d the formation of inactive long-chain polymers. Serpin polymerization not only
reduces the amount of active inhibitor, but also leads to accumulation of the po
lymers, which can cause cell death and even organ failure. (Serpins are a superf
amily of proteins with similar structures that were first recognized for their p
rotease inhibition activity and are found in all kingdoms of life. Their unusual
mechanism of action irreversibly inhibits their target protease by undergoing a
large conformational change to disrupt its active site. This contrasts with the
more common competitive mechanism for protease inhibitors that bind to and bloc
k access to the protease active site. Protease inhibition by serpins controls an
array of biological processes, including coagulation and inflammation, and cons
equently these proteins are the target of medical research. Their conformational

-change mechanism confers certain advantages, but it also has drawbacks: serpins
are vulnerable to mutations that can result in protein misfolding and the forma
tion of inactive long-chain polymers. Serpin polymerization not only reduces the
amount of active inhibitor, but also leads to accumulation of the polymers, whi
ch can cause cell death and even organ failure. (Serpins are a superfamily of pr
oteins with similar structures that were first recognized for their protease inh
ibition activity and are found in all kingdoms of life. Their unusual mechanism
of action irreversibly inhibits their target protease by undergoing a large conf
ormational change to disrupt its active site. This contrasts with the more commo
n competitive mechanism for protease inhibitors that bind to and block access to
the protease active site. Protease inhibition by serpins controls an array of b
iological processes, including coagulation and inflammation, and consequently th
ese proteins are the target of medical research. Their conformational-change mec
hanism confers certain advantages, but it also has drawbacks: serpins are vulner
able to mutations that can result in protein misfolding and the formation of ina
ctive long-chain polymers. Serpin polymerization not only reduces the amount of
active inhibitor, but also leads to accumulation of the polymers, which can caus
e cell death and even organ failure. (Serpins are a superfamily of proteins with
similar structures that were first recognized for their protease inhibition act
ivity and are found in all kingdoms of life. Their unusual mechanism of action i
rreversibly inhibits their target protease by undergoing a large conformational
change to disrupt its active site. This contrasts with the more common competiti
ve mechanism for protease inhibitors that bind to and block access to the protea
se active site. Protease inhibition by serpins controls an array of biological p
rocesses, including coagulation and inflammation, and consequently these protein
s are the target of medical research. Their conformational-change mechanism conf
ers certain advantages, but it also has drawbacks: serpins are vulnerable to mut
ations that can result in protein misfolding and the formation of inactive longchain polymers. Serpin polymerization not only reduces the amount of active inhi
bitor, but also leads to accumulation of the polymers, which can cause cell deat
h and even organ failure. (Serpins are a superfamily of proteins with similar st
ructures that were first recognized for their protease inhibition activity and a
re found in all kingdoms of life. Their unusual mechanism of action irreversibly
inhibits their target protease by undergoing a large conformational change to d
isrupt its active site. This contrasts with the more common competitive mechanis
m for protease inhibitors that bind to and block access to the protease active s
ite. Protease inhibition by serpins controls an array of biological processes, i
ncluding coagulation and inflammation, and consequently these proteins are the t
arget of medical research. Their conformational-change mechanism confers certain
advantages, but it also has drawbacks: serpins are vulnerable to mutations that
can result in protein misfolding and the formation of inactive long-chain polym
ers. Serpin polymerization not only reduces the amount of active inhibitor, but
also leads to accumulation of the polymers, which can cause cell death and even
organ failure. (Serpins are a superfamily of proteins with similar structures th
at were first recognized for their protease inhibition activity and are found in
all kingdoms of life. Their unusual mechanism of action irreversibly inhibits t
heir target protease by undergoing a large conformational change to disrupt its
active site. This contrasts with the more common competitive mechanism for prote
ase inhibitors that bind to and block access to the protease active site. Protea
se inhibition by serpins controls an array of biological processes, including co
agulation and inflammation, and consequently these proteins are the target of me
dical research. Their conformational-change mechanism confers certain advantages
, but it also has drawbacks: serpins are vulnerable to mutations that can result
in protein misfolding and the formation of inactive long-chain polymers. Serpin
polymerization not only reduces the amount of active inhibitor, but also leads
to accumulation of the polymers, which can cause cell death and even organ failu
re. (Serpins are a superfamily of proteins with similar structures that were fir
st recognized for their protease inhibition activity and are found in all kingdo
ms of life. Their unusual mechanism of action irreversibly inhibits their target
protease by undergoing a large conformational change to disrupt its active site

. This contrasts with the more common competitive mechanism for protease inhibit
ors that bind to and block access to the protease active site. Protease inhibiti
on by serpins controls an array of biological processes, including coagulation a
nd inflammation, and consequently these proteins are the target of medical resea
rch. Their conformational-change mechanism confers certain advantages, but it al
so has drawbacks: serpins are vulnerable to mutations that can result in protein
misfolding and the formation of inactive long-chain polymers. Serpin polymeriza
tion not only reduces the amount of active inhibitor, but also leads to accumula
tion of the polymers, which can cause cell death and even organ failure. (Serpin
s are a superfamily of proteins with similar structures that were first recogniz
ed for their protease inhibition activity and are found in all kingdoms of life.
Their unusual mechanism of action irreversibly inhibits their target protease b
y undergoing a large conformational change to disrupt its active site. This cont
rasts with the more common competitive mechanism for protease inhibitors that bi
nd to and block access to the protease active site. Protease inhibition by serpi
ns controls an array of biological processes, including coagulation and inflamma
tion, and consequently these proteins are the target of medical research. Their
conformational-change mechanism confers certain advantages, but it also has draw
backs: serpins are vulnerable to mutations that can result in protein misfolding
and the formation of inactive long-chain polymers. Serpin polymerization not on
ly reduces the amount of active inhibitor, but also leads to accumulation of the
polymers, which can cause cell death and even organ failure. (Serpins are a sup
erfamily of proteins with similar structures that were first recognized for thei
r protease inhibition activity and are found in all kingdoms of life. Their unus
ual mechanism of action irreversibly inhibits their target protease by undergoin
g a large conformational change to disrupt its active site. This contrasts with
the more common competitive mechanism for protease inhibitors that bind to and b
lock access to the protease active site. Protease inhibition by serpins controls
an array of biological processes, including coagulation and inflammation, and c
onsequently these proteins are the target of medical research. Their conformatio
nal-change mechanism confers certain advantages, but it also has drawbacks: serp
ins are vulnerable to mutations that can result in protein misfolding and the fo
rmation of inactive long-chain polymers. Serpin polymerization not only reduces
the amount of active inhibitor, but also leads to accumulation of the polymers,
which can cause cell death and even organ failure. (Serpins are a superfamily of
proteins with similar structures that were first recognized for their protease
inhibition activity and are found in all kingdoms of life. Their unusual mechani
sm of action irreversibly inhibits their target protease by undergoing a large c
onformational change to disrupt its active site. This contrasts with the more co
mmon competitive mechanism for protease inhibitors that bind to and block access
to the protease active site. Protease inhibition by serpins controls an array o
f biological processes, including coagulation and inflammation, and consequently
these proteins are the target of medical research. Their conformational-change
mechanism confers certain advantages, but it also has drawbacks: serpins are vul
nerable to mutations that can result in protein misfolding and the formation of
inactive long-chain polymers. Serpin polymerization not only reduces the amount
of active inhibitor, but also leads to accumulation of the polymers, which can c
ause cell death and even organ failure. (Serpins are a superfamily of proteins w
ith similar structures that were first recognized for their protease inhibition
activity and are found in all kingdoms of life. Their unusual mechanism of actio
n irreversibly inhibits their target protease by undergoing a large conformation
al change to disrupt its active site. This contrasts with the more common compet
itive mechanism for protease inhibitors that bind to and block access to the pro
tease active site. Protease inhibition by serpins controls an array of biologica
l processes, including coagulation and inflammation, and consequently these prot
eins are the target of medical research. Their conformational-change mechanism c
onfers certain advantages, but it also has drawbacks: serpins are vulnerable to
mutations that can result in protein misfolding and the formation of inactive lo
ng-chain polymers. Serpin polymerization not only reduces the amount of active i
nhibitor, but also leads to accumulation of the polymers, which can cause cell d

eath and even organ failure. (Serpins are a superfamily of proteins with similar
structures that were first recognized for their protease inhibition activity an
d are found in all kingdoms of life. Their unusual mechanism of action irreversi
bly inhibits their target protease by undergoing a large conformational change t
o disrupt its active site. This contrasts with the more common competitive mecha
nism for protease inhibitors that bind to and block access to the protease activ
e site. Protease inhibition by serpins controls an array of biological processes
, including coagulation and inflammation, and consequently these proteins are th
e target of medical research. Their conformational-change mechanism confers cert
ain advantages, but it also has drawbacks: serpins are vulnerable to mutations t
hat can result in protein misfolding and the formation of inactive long-chain po
lymers. Serpin polymerization not only reduces the amount of active inhibitor, b
ut also leads to accumulation of the polymers, which can cause cell death and ev
en organ failure. (Serpins are a superfamily of proteins with similar structures
that were first recognized for their protease inhibition activity and are found
in all kingdoms of life. Their unusual mechanism of action irreversibly inhibit
s their target protease by undergoing a large conformational change to disrupt i
ts active site. This contrasts with the more common competitive mechanism for pr
otease inhibitors that bind to and block access to the protease active site. Pro
tease inhibition by serpins controls an array of biological processes, including
coagulation and inflammation, and consequently these proteins are the target of
medical research. Their conformational-change mechanism confers certain advanta
ges, but it also has drawbacks: serpins are vulnerable to mutations that can res
ult in protein misfolding and the formation of inactive long-chain polymers. Ser
pin polymerization not only reduces the amount of active inhibitor, but also lea
ds to accumulation of the polymers, which can cause cell death and even organ fa
ilure. (Serpins are a superfamily of proteins with similar structures that were
first recognized for their protease inhibition activity and are found in all kin
gdoms of life. Their unusual mechanism of action irreversibly inhibits their tar
get protease by undergoing a large conformational change to disrupt its active s
ite. This contrasts with the more common competitive mechanism for protease inhi
bitors that bind to and block access to the protease active site. Protease inhib
ition by serpins controls an array of biological processes, including coagulatio
n and inflammation, and consequently these proteins are the target of medical re
search. Their conformational-change mechanism confers certain advantages, but it
also has drawbacks: serpins are vulnerable to mutations that can result in prot
ein misfolding and the formation of inactive long-chain polymers. Serpin polymer
ization not only reduces the amount of active inhibitor, but also leads to accum
ulation of the polymers, which can cause cell death and even organ failure. (Ser
pins are a superfamily of proteins with similar structures that were first recog
nized for their protease inhibition activity and are found in all kingdoms of li
fe. Their unusual mechanism of action irreversibly inhibits their target proteas
e by undergoing a large conformational change to disrupt its active site. This c
ontrasts with the more common competitive mechanism for protease inhibitors that
bind to and block access to the protease active site. Protease inhibition by se
rpins controls an array of biological processes, including coagulation and infla
mmation, and consequently these proteins are the target of medical research. The
ir conformational-change mechanism confers certain advantages, but it also has d
rawbacks: serpins are vulnerable to mutations that can result in protein misfold
ing and the formation of inactive long-chain polymers. Serpin polymerization not
only reduces the amount of active inhibitor, but also leads to accumulation of
the polymers, which can cause cell death and even organ failure. (Serpins are a
superfamily of proteins with similar structures that were first recognized for t
heir protease inhibition activity and are found in all kingdoms of life. Their u
nusual mechanism of action irreversibly inhibits their target protease by underg
oing a large conformational change to disrupt its active site. This contrasts wi
th the more common competitive mechanism for protease inhibitors that bind to an
d block access to the protease active site. Protease inhibition by serpins contr
ols an array of biological processes, including coagulation and inflammation, an
d consequently these proteins are the target of medical research. Their conforma

tional-change mechanism confers certain advantages, but it also has drawbacks: s

erpins are vulnerable to mutations that can result in protein misfolding and the
formation of inactive long-chain polymers. Serpin polymerization not only reduc
es the amount of active inhibitor, but also leads to accumulation of the polymer
s, which can cause cell death and even organ failure. (Serpins are a superfamily
of proteins with similar structures that were first recognized for their protea
se inhibition activity and are found in all kingdoms of life. Their unusual mech
anism of action irreversibly inhibits their target protease by undergoing a larg
e conformational change to disrupt its active site. This contrasts with the more
common competitive mechanism for protease inhibitors that bind to and block acc
ess to the protease active site. Protease inhibition by serpins controls an arra
y of biological processes, including coagulation and inflammation, and consequen
tly these proteins are the target of medical research. Their conformational-chan
ge mechanism confers certain advantages, but it also has drawbacks: serpins are
vulnerable to mutations that can result in protein misfolding and the formation
of inactive long-chain polymers. Serpin polymerization not only reduces the amou
nt of active inhibitor, but also leads to accumulation of the polymers, which ca
n cause cell death and even organ failure. (Serpins are a superfamily of protein
s with similar structures that were first recognized for their protease inhibiti
on activity and are found in all kingdoms of life. Their unusual mechanism of ac
tion irreversibly inhibits their target protease by undergoing a large conformat
ional change to disrupt its active site. This contrasts with the more common com
petitive mechanism for protease inhibitors that bind to and block access to the
protease active site. Protease inhibition by serpins controls an array of biolog
ical processes, including coagulation and inflammation, and consequently these p
roteins are the target of medical research. Their conformational-change mechanis
m confers certain advantages, but it also has drawbacks: serpins are vulnerable
to mutations that can result in protein misfolding and the formation of inactive
long-chain polymers. Serpin polymerization not only reduces the amount of activ
e inhibitor, but also leads to accumulation of the polymers, which can cause cel
l death and even organ failure. (Serpins are a superfamily of proteins with simi
lar structures that were first recognized for their protease inhibition activity
and are found in all kingdoms of life. Their unusual mechanism of action irreve
rsibly inhibits their target protease by undergoing a large conformational chang
e to disrupt its active site. This contrasts with the more common competitive me
chanism for protease inhibitors that bind to and block access to the protease ac
tive site. Protease inhibition by serpins controls an array of biological proces
ses, including coagulation and inflammation, and consequently these proteins are
the target of medical research. Their conformational-change mechanism confers c
ertain advantages, but it also has drawbacks: serpins are vulnerable to mutation
s that can result in protein misfolding and the formation of inactive long-chain
polymers. Serpin polymerization not only reduces the amount of active inhibitor
, but also leads to accumulation of the polymers, which can cause cell death and
even organ failure. (Serpins are a superfamily of proteins with similar structu
res that were first recognized for their protease inhibition activity and are fo
und in all kingdoms of life. Their unusual mechanism of action irreversibly inhi
bits their target protease by undergoing a large conformational change to disrup
t its active site. This contrasts with the more common competitive mechanism for
protease inhibitors that bind to and block access to the protease active site.
Protease inhibition by serpins controls an array of biological processes, includ
ing coagulation and inflammation, and consequently these proteins are the target
of medical research. Their conformational-change mechanism confers certain adva
ntages, but it also has drawbacks: serpins are vulnerable to mutations that can
result in protein misfolding and the formation of inactive long-chain polymers.
Serpin polymerization not only reduces the amount of active inhibitor, but also
leads to accumulation of the polymers, which can cause cell death and even organ
failure. (vv