What causes proteins denature?

Detergent are both cationic and or anionic. Denaturation of protein eans inactivation too. Its like the activity of protein decreases due to denaturation but still the backbone of protein remains intact. Detergents can be denaturing or non-denaturing with respect to protein structure. Denaturing detergents can be anionic such as sodium dodecyl sulfate (SDS) or cationic such as ethyl trimethyl ammonium bromide. These detergents totally denaturate proteins by breaking protein–protein interactions. Proteins are active in their 3D structure and to maintain that 3D sturcture hydrogen bond, hydrophobic interactions, salt bridges, electrostatic interactions etc are very important. While due to charged mature of detergents they disturb the intra- molecular interactions by forming temporary bonds between them and leads to breaking of 3D structure so protein can not work. So its like detergents provide relaxation to proteins and so they are unable to work like holidays does no us. Changes in pH affect the chemistry of amino acid residues and can lead to denaturation. ... Protonation of the amino acid residues (when an acidic proton H attaches to a lone pair of electrons on a nitrogen) changes whether or not they participate in hydrogen bonding, so a change in the pH can denature a protein. Heat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted. The proteins in eggs denature and coagulate during cooking. #aminoAcids #proteins #popypeptides #ologopeptides #peptides #NikolaysGeneticsLessons #protein #polypeptide #aminoAcid #peptide #disulfideBridges #covalentBounding #ionicBounding #hydrophobicInteraction #proteinStructure #proteinSequence #proteinFolding #Polypeptides #ImidazolRing #Histidine #polypeptideChain #oligopeptide #hydrolysesSynthesis #condensationReaction #globularProteins #fibrousProteins #Genetics