Medical College of Wisconsin
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Refolding a disulfide dimer of cytochrome c. Biochemistry 1985 Jul 02;24(14):3459-64

Date

07/02/1985

Pubmed ID

2994710

DOI

10.1021/bi00335a011

Scopus ID

2-s2.0-0022417662 (requires institutional sign-in at Scopus site)   19 Citations

Abstract

A covalent dimer of Saccharomyces cerevisiae iso-1 cytochrome c is stabilized by an interchain disulfide bond involving the cysteine residue penultimate to the C-terminus. The individual chains in the dimer appear to retain the tertiary structural features characteristic for monomeric cytochrome c albeit with some perturbation. The dimer is reversibly denatured by heat, urea, or guanidine hydrochloride in a single cooperative transition whose midpoint is less than that of the monomeric protein. The kinetic profile observed for the refolding of the denatured dimer is characteristic for monomeric cytochromes except for a markedly enhanced slow-phase amplitude.

Author List

Bryant C, Strottmann JM, Stellwagen E

Author

James M. Strottmann MD Associate Professor in the Radiology department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Circular Dichroism
Cytochrome c Group
Disulfides
Guanidine
Guanidines
Kinetics
Macromolecular Substances
Protein Conformation
Protein Denaturation
Saccharomyces cerevisiae
Urea