Salt bridges in proteins

Salt bridges in proteins are bonds between oppositely charged residues that are sufficiently close to each other to experience electrostatic attraction. They contribute to protein structure and to the specificity of interaction of proteins with other biomolecules, but in doing so they need not necessarily increase a protein’s free energy of unfolding. The salt bridge most often arises from the anionic carboxylate (RCOO−) of either aspartic acid or glutamic acid and the cationic ammonium (RNH3 ) from lysine or the guanidinium (RNHC(NH2)2 ) of arginine. Salt bridges: A) Form when oppositely-charged amino acid side chains contact each other B) Form when positively charged amino acid side chains contact each other C) Form mostly in the core of the molecule D) Form mostly on the surface of the molecule E) Are covalent bonds #saltBridges #proteins #aminoAcids #polypeptideChain #NikolaysGeneticsLessons #protein #polypeptide #aminoAcid #peptide #disulfideBridges #covalentBounding #ionicBounding #hydrophobicInteraction #proteinStructure #proteinSequence #proteinFolding #Polypeptides #ImidazolRing #Histidine #oligopeptide #hydrolysesSynthesis #condensationReaction #condensationSynthesis #peptides #globularProteins #fibrousProteins