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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Investigating Mechanisms of Collagen Thermal Denaturation by High Resolution Second-Harmonic Generation Imaging
Oct 01, 2006; ABSTRACT We apply the technique of second-harmonic generation (SHG) microscopy to obtain large area submicron resolution image of...
Pressure Denaturation of Staphylococcal Nuclease Studied by Neutron Small-Angle Scattering and Molecular Simulation
Nov 01, 2004; ABSTRACT We studied the pressure-induced folding/unfolding transition of staphylococcal nuclease (SN) over a pressure range of...