GENERAL PROPERTIES OF PROTEINS

• Taste: They are tasteless. However, the hydrolytic pro- ducts (derived
proteins) are bitter in taste. 


• Odour: They are odourless. When heated to dryness they turn brown and
give off the odour of burning feather. 


• Molecular weight: The proteins in general have a large molecular weight.

Proteins therefore are macromolecules. Molecular weight is determined
by physical methods such as osmotic pressure measure- ment,
depression in freezing point, light scattering effect, X-ray diffraction,
turbidity measurement and now by methods such as analytical
ultracentri- fugation, molecular sieving by gel filtration and SDS-
polyacrylamide gel electrophoresis. Mol. Wt. of some common proteins
is shown in Table 6.1. 


• Viscosity of protein solutions: The viscosity of protein varies widely with the
kind of protein and its concentration in solution. The viscosity is closely related to
molecular shape, long molecules (fibrous proteins) being more viscous than globular
proteins. Thus fibrinogen can form a more viscous solution than albumin.

• Hydration of proteins: Polar groups of proteins such as -NH2 and -COOH

become hydrated in presence of water and swell up when electrolytes, alcohol or
sugars that form complexes with water are added to
proteinsolutions.Thereiscompetitionforwater and the degree of hydration of
protein is decreased. They dehydrate protein and precipitate it from solution.

• Heat coagulation of proteins: Several proteins coagulate forming an insoluble

coagulum. Coagu- lation is maximum at the isoelectric pH of the protein. During
coagulation, protein undergoes a change called as denaturation. Denatured
proteins are soluble in extremes of pH and maximum precipitation occurs at isoelectric
pH (pI) of the protein.

• Amphoteric nature of proteins: In any protein molecule there are amino acids
which carry -COOH or -NH2 groups in their side chains. These groups can
undergo ionisation in solution producing both anions and cations. In addition to
the side chains of polar amino acids, N-terminal -NH2 group and C-terminal -
COOH group may also ionise. Depending on the pH few groups act as proton
donors while few as proton acceptors. Therefore proteins are ampholytes and act both
as acids and bases. At a specific pH called an isoelectric pH (pI) a protein exists as a
dipolar ion or “Zwitterion” or “Hybrid” ion, carrying equal number of positive and
negative charges on its ionizable groups. So the net charge on protein molecule at its
isoelectric pH is zero.

On the acidic side of its isoelectric pH, a protein exists as a cation by accepting a
proton and migrates towards anode in an electrical field; while on the alka- line
side of its pI a protein exists as anion by donating a proton and migrates towards
cathode. This property is made use of in electrophoresis to separate different
proteins depending on the charge present in them at a particular pH.

• Precipitation of proteins: Proteins can be precipitated from solutions by a

variety of +ve and –ve ions. Such precipitation is of importance in the isolation of
protein, in the deproteinisation of blood and other biological fluids and extracts
for analysis and in the preparation of useful protein derivatives.