Role of Protein Stabilizers on the Conformation of the Unfolded State of Cytochrome c and Its Early Folding Kinetics
Open Access
- 1 August 2010
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 285 (33) , 25314-25323
Abstract
No abstract availableKeywords
This publication has 60 references indexed in Scilit:
- Direct observation of ultrafast folding and denatured state dynamics in single protein moleculesProceedings of the National Academy of Sciences, 2009
- Direct evidence for a dry molten globule intermediate during the unfolding of a small proteinProceedings of the National Academy of Sciences, 2009
- Early Events, Kinetic Intermediates and the Mechanism of Protein Folding in Cytochrome cInternational Journal of Molecular Sciences, 2009
- Inhibition of Protein Aggregation: Supramolecular Assemblies of Arginine Hold the KeyPLOS ONE, 2007
- Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopyProceedings of the National Academy of Sciences, 2007
- A molecular mechanism for osmolyte-induced protein stabilityProceedings of the National Academy of Sciences, 2006
- A two-dimensional view of the folding energy landscape of cytochrome cProceedings of the National Academy of Sciences, 2006
- Kinetics of Loop Formation and Breakage in the Denatured State of Iso-1-cytochrome cJournal of Molecular Biology, 2005
- The Cytochrome c Folding Landscape Revealed by Electron-transfer KineticsJournal of Molecular Biology, 2002
- Denatured state thermodynamics: residual structure, chain stiffness and scaling factors11Edited by C. R. MatthewsJournal of Molecular Biology, 2001