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Protein
2314100095 M.Aziz Rahmatullah
2314100135 Dany Destyawan Anwar
2315100047 Surya Aji Prasetya
02211748007002 Fatin Fatihah
PROTEINS
• Proteins are polymers of amino acids linked
together by peptide bonds.
• Two or more amino acids joined together are
called a polypeptide, while molecules that consist
of one or more polypeptides are termed proteins.
AMINO ACIDS
THE BUILDING BLOCKS OF PROTEINS
Hydrophobic core
Hydrophilic surface
DENATURED
Fast under non-physiological conditions
NATIVE
Exposure to acids or alkalis (i.e. pH changes) affects the overall net charge on a
protein, which will change the extent of electrostatic interactions, both
attractive and repulsive. Most proteins are stable within a pH range around
their isoelectric point (zero net charge) and the effects of acids or alkalis are
normally reversible.
• Heavy Metal salts
Usually contain Hg, Pb, Ag, TI, Cd, and other high atomic weights. Since salts are ionic they distrupt
salt bridges in protein. The Reaction of a Heavy metal salt with protein usually leads to an insoluble
metal protein salts. As for example AgNO3 is used to prevent gonorrhea infection.
• Detergents
Hydrophobic parts of detergent associate with hydrophobic parts of the protein which dissociating
hydrophobic parts of protein that no longer associating with other that can lead to unfolding of
protein chain.
• Organic Solvent
weakens hydrophobic interactions since non-polar side chains become more soluble. Organic
solutes can have a variety of effects. Urea alters the structure of water in such a way as to weaken
hydrophobic interactions, leading to protein unfolding
Protein Purification
The critical study of food protein structure and function
is the ability to purify protein. Separating a particular
protein from a complex mixture of many proteins, often
hundreds or thousands, is done by taking advantage of
differing biochemical characteristics such as charge, pI,
mass, molecular shape and size, hydrophobicity, ligand
affinity, and enzymatic activity among others.
3. While the smaller proteins that enter and exit beads take a more convoluted
longer path.
4. Hence larger proteins elute before smaller proteins in size exclusion
chromatography, thereby allowing for the separation of many proteins within a
mixture based on size.
SIZE EXCLUSION CHROMATOGRAPHY
The resolution for separation of masses varies with :
1. Quality of setup purchased
2. Length of the column.