Structural Characterization of an Equilibrium Unfolding Intermediate in Cytochrome c
Authors:
- 1 March 2006
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 357 (3) , 1009-1025
Abstract
No abstract availableKeywords
Funding Information
- National Science Foundation (MCB-079148)
- National Institutes of Health (CA06927, GM056250)
This publication has 84 references indexed in Scilit:
- Kinetics of Loop Formation and Breakage in the Denatured State of Iso-1-cytochrome cJournal of Molecular Biology, 2005
- Early Events During Folding of Wild-type Staphylococcal Nuclease and a Single-tryptophan Variant Studied by Ultrarapid MixingJournal of Molecular Biology, 2004
- Two-state expansion and collapse of a polypeptideJournal of Molecular Biology, 2000
- Cytochrome c folding traps are not due solely to histidine-heme ligation: direct demonstration of a role for N-terminal amino group-heme ligation 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Global Analysis of the Acid-Induced and Urea-Induced Unfolding of Staphylococcal Nuclease and Two of Its VariantsBiochemistry, 1997
- A Lysine 73 → Histidine Variant of Yeast Iso-1-cytochrome c: Evidence for a Native-like Intermediate in the Unfolding Pathway and Implications for m Value EffectsBiochemistry, 1997
- Intermediate States in Protein FoldingJournal of Molecular Biology, 1996
- Role of Heme Axial Ligands in the Conformational Stability of the Native and Molten Globule States of Horse CytochromeJournal of Molecular Biology, 1996
- How does a protein fold?Nature, 1994
- Kinetics of unfolding and refolding of proteinsJournal of Molecular Biology, 1973