title: Evidence for an unfolding and refolding pathway in cytochrome c.
abstract: It has been suggested that three partially unfolded forms detected in a native state hydrogen exchange study of oxidized cytochrome c may represent sequential intermediates in an unfolding-refolding pathway. To better define the structure of each intermediate a 'stability labeling' method was used in which the stability of a given segment against unfolding was changed. The condition--folded or unfolded--of the stability-labeled segment in each intermediate could then be determined. The structures found are discrete and native-like and are just those necessary for a sequential pathway.
authors.affiliation: Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Xu
authors.forename: L
authors.initials: L
authors.lastname: Mayne
authors.forename: S W
authors.initials: SW
authors.lastname: Englander
mesh_terms: D000818:Animals; D001665:Binding Sites; D003574:Cytochrome c Group / Q000737:chemistry*; D006418:Heme / Q000737:chemistry; D006736:Horses; D006859:Hydrogen / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008715:Methionine / Q000737:chemistry; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D003574:Cytochrome c Group; D006418:Heme; D006859:Hydrogen; D008715:Methionine