BSC 2010C Lecture 1: Bio Notes 223 - Disulfide Bridges
Document Summary
Disulfide bridges, also known as disulfide bonds, are covalent bonds formed between two cysteine amino acid residues in a protein. Cysteine is unique among the 20 amino acids commonly found in proteins because it has a sulfur-containing group in its side chain that can react with another cysteine residue to form a disulfide bond. Disulfide bridges are important for stabilizing the three-dimensional structure of proteins. When two cysteine residues come close enough together, the sulfur atoms on each cysteine react with each other to form a covalent bond, resulting in a loop of protein structure that is held together by the disulfide bridge. These bridges are particularly important in proteins that are secreted from cells or reside in extracellular spaces, where they are exposed to a variety of environmental conditions. Disulfide bridges can have a major impact on the properties and functions of proteins. They can contribute to protein stability, protect against proteolytic degradation, and influence protein-protein interactions.
