Effects of Heme on the Structure of the Denatured State and Folding Kinetics of Cytochrome b562-Reference-Cited by-同舟云学术

Effects of Heme on the Structure of the Denatured State and Folding Kinetics of Cytochrome b562

Published:2005-02 Issue:1 Volume:346 Page:331-344
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Garcia Pascal,Bruix Marta,Rico Manuel,Ciofi-Baffoni Simone,Banci Lucia,Ramachandra Shastry M.C.,Roder Heinrich,de Lumley Woodyear Thierry,Johnson Christopher M.,Fersht Alan R.,Barker Paul. D.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference51 articles.

1. Role of cofactors in protein folding;Wittung-Stafshede;Accts Chem. Res.,2002

2. A surprising simplicity to protein folding;Baker;Nature,2000

3. Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics;Plaxco;Biochemistry,2000

4. The conformation of horse heart apocytochrome c;Stellwagen;J. Biol. Chem.,1972

5. Still a puzzle: why is haem covalently attached in c-type cytochromes?;Barker;Structure,1999

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