title: How do cofactors modulate protein folding?
abstract: Cofactors are essential components of many proteins for biological activity. Characterization of several cofactor-binding proteins has shown that cofactors often have the ability to interact specifically with the unfolded polypeptides. This suggests that cofactor-coordination prior to polypeptide folding may be a relevant path in vivo. By binding before folding, the cofactor may affect both the mechanism and speed of folding. Here, we discuss three different cofactors that modulate protein-folding processes in vitro.
authors.affiliation: Chemistry Department, Tulane University, New Orleans, Louisiana 70118, USA.
authors.forename: Catherine L
authors.initials: CL
authors.lastname: Higgins
authors.forename: B K
authors.initials: BK
authors.lastname: Muralidhara
authors.forename: Pernilla
authors.initials: P
authors.lastname: Wittung-Stafshede
mesh_terms: D000818:Animals; D001400:Azurin / Q000737:chemistry / Q000378:metabolism; D003067:Coenzymes / Q000737:chemistry* / Q000378:metabolism; D005288:Ferredoxins / Q000737:chemistry / Q000378:metabolism; D005418:Flavodoxin / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008670:Metals / Q000737:chemistry; D008958:Models, Molecular; D017510:Protein Folding; D020836:Protein Structure, Quaternary
chemical_list: D003067:Coenzymes; D005288:Ferredoxins; D005418:Flavodoxin; D008670:Metals; D001400:Azurin