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1. Denaturation:
Partial or complete unfolding of the native (natural) conformation of the polypeptide
chain is known as denaturation. This is caused by heat, acids, alkalies, alcohol,
acetone, urea, beta- mercaptoethanol.
2. Coagulation:
When proteins are denatured by heat, they form insoluble aggregates known as
coagulum. All the proteins are not heat coagulable, only a few like the albumins,
globulins are heat coagulable.
3. Isoelectric pH (pH1):
The pH at which a protein has equal number of positive and negative charges is
known as isoelectric pH. When subjected to an electric field the proteins do not move
either towards anode or cathode, hence this property is used to isolate proteins. The
proteins become least soluble at pHI and get precipitated. The pHI of casein is 4.5 and
at this pH the casein in milk curdles producing the curd.
4. Molecular Weights of Proteins:
The average molecular weight of an amino acid is taken to be 110. The total number
of amino acids in a protein multiplied by 110 gives the approximate molecular weight
of that protein. Different proteins have different amino acid composition and hence
their molecular weights differ. The molecular weights of proteins range from 5000 to
109 Daltons. Experimentally the molecular weight can be determined by methods like
gel filtration, PAGE, ultra-centrifugation or viscosity measurements.
Anganifelix answered the question on May 9, 2018 at 17:13
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