How Cytochrome c Folds, and Why: Submolecular Foldon Units and their Stepwise Sequential Stabilization
- 1 October 2004
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 343 (1) , 223-233
- https://doi.org/10.1016/j.jmb.2004.08.005
Abstract
No abstract availableKeywords
This publication has 63 references indexed in Scilit:
- Conformational Heterogeneity of an Equilibrium Folding Intermediate Quantified and Mapped by Scanning MutagenesisJournal of Molecular Biology, 2004
- The equilibrium unfolding pathway of a (β/α)8 barrelJournal of Molecular Biology, 2002
- On the nature of conformational openings: native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobinJournal of Molecular Biology, 2001
- Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobinJournal of Molecular Biology, 1999
- Experimental study of the protein folding landscape: unfolding reactions in cytochrome cJournal of Molecular Biology, 1999
- Evidence for an unfolding and refolding pathway in cytochrome cNature Structural & Molecular Biology, 1998
- Two forms of the pH 4 folding intermediate of apomyoglobinJournal of Molecular Biology, 1998
- Structures of folding intermediatesCurrent Opinion in Structural Biology, 1995
- Stable submolecular folding units in a non-compact form of cytochrome cJournal of Molecular Biology, 1991
- Proton resonance assignments of horse ferricytochrome cBiochemistry, 1989