Not one, but many forms of thrombosis proteins.

The disulfide bond is a covalent bond formed between the sulfur atoms of two cysteine residues in proteins. Our understanding of the role of these ubiquitous bonds in protein function has changed dramatically over the past decade. Initially thought to be fully formed and inert in the native protein, we know now that both these assumptions are incorrect for many proteins. Here, we review recent evidence for production and function of multiple partially disulfide-bonded forms of plasma fibrinogen and platelet αIIbβ3 integrin. The disulfide bonds are not cleaved in these mature proteins but rather a significant fraction of the bonds never form during maturation of the protein. The resulting different covalent states influence the functioning of the protein. These findings change our concept of the native, functional protein.