Proteins are responsible for all of life's processes and their structure is defined by two main types of covalent bonds: the peptide bonds that link the amino acid residues and disulfide bonds that link pairs of cysteine amino acids. Since the identification of disulfide bonds in the early 1960's they were long thought to be fully formed and inert in the mature protein.
Disulfide bond control of protein function
Disulfide bond regulation of protein function is being observed across biological systems and lifeforms. The Hogg Lab focuses on elucidating disulfide bond control of blood clotting and autoimmunity.
The Hogg Lab has shown that disulfide bonds are neither fully formed nor inert in proteins. Many proteins are constitutively produced and function as an array of partially disulfide-bonded states, and a subset of the formed disulfides – the allosteric disulfides – are cleaved by different factors to control mature protein function.