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Protein Denaturation

Definition

The loss of a protein's three-dimensional structure without breaking peptide bonds, caused by heat, pH change, UV radiation, or chemical agents such as strong detergents. Denaturation destroys biological activity because function depends on shape. In forensic samples, denaturation reduces the sensitivity of enzyme-based assays.

Related terms

Amino Acid
The monomer unit of proteins. All 20 standard amino acids share a central carbon bonded to an amino group, a carboxyl group,...
Haemichrome
A further oxidation product formed when the globin chains of methaemoglobin denature and the haem group becomes internally coordinated. Associated with the...
Haemoglobin
The iron-containing oxygen-transport protein in red blood cells, composed of four polypeptide subunits each with a haem prosthetic group. Its pseudoperoxidase activity...
Isoenzyme (Isozyme)
Multiple molecular forms of the same enzyme that differ in amino acid sequence but catalyse the same reaction. In forensic serology, isoenzyme...
Methaemoglobin
An oxidised form of haemoglobin in which ferrous iron (Fe2+) is converted to ferric iron (Fe3+), unable to carry oxygen. Its formation...
Oxyhaemoglobin
The form of haemoglobin in freshly shed arterial blood, where iron in the haem group is in the ferrous (Fe²⁺) state and...
Peroxidase
An enzyme that catalyses the transfer of oxygen from hydrogen peroxide to an electron donor, often producing a coloured product. Haemoglobin has...
Photodegradation
Breakdown of biological molecules driven by ultraviolet and visible radiation. In bloodstains it accelerates haemoglobin oxidation and cleaves DNA strands, hastening ageing...
Proteolysis
The hydrolytic cleavage of peptide bonds by proteolytic enzymes (proteases). In biological evidence, proteolysis occurs via endogenous cellular proteases released during autolysis...
Substrate Effect
The influence of the surface on which a bloodstain lies on the rate and character of chemical change. Porous substrates absorb blood...

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