Biochemical process modifying a protein's natural configuration. It involves breaking many weak (hydrogen and hydrophobic) bonds (see bonding) that maintain the protein's highly ordered structure. This usually results in loss of biological activity (e.g., loss of an enzyme's ability to catalyze reactions). Denaturation can be brought about by heating; treatment with alkalis, acids, urea, or detergents; or even vigorous shaking of the protein solution. It can be reversed in some cases (e.g., serum albumin, hemoglobin), if conditions favourable to the protein are restored, but not in others. The term is also used to describe the process of rendering ethanol unfit to drink.
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