DENATURATION OF PROTEIN
Denaturation of Protein
- Distruption of higher structures of protein (Primary, secondary and tertiary).
- During denaturation, peptide bond remains intact.
- Denaturation can completely disrupt secondary, tertiary and quaternary structures.
- Denatuartion is irreversible.
- Denaturation is randamization of conformation of polypeptide chain.
- Denaturation is always accompanied by loss of biological function.
- Dentatured proteins are less soluble and they precipitate.
- Denaturation agents are- 8M urea or 6 M guanidine chloride.
- Denaturation assume a random coil structure.
Exam Important
- Distruption of higher structures of protein (Primary, secondary and tertiary).
- During denaturation, peptide bond remains intact.
- Denaturation can completely disrupt secondary, tertiary and quaternary structures.
- Denatuartion is irreversible.
- Denaturation is randamization of conformation of polypeptide chain.
- Denaturation is always accompanied by loss of biological function.
- Dentatured proteins are less soluble and they precipitate.
- Denaturation agents are- 8M urea or 6 M guanidine chloride.
- Denaturation assume a random coil structure.
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