Discerning the Structure and Energy of Multiple Transition States in Protein Folding using ψ-Analysis
- 19 March 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 337 (2) , 463-475
- https://doi.org/10.1016/j.jmb.2004.01.018
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein foldingPublished by Elsevier ,2004
- Origin of Unusual φ-values in Protein Folding: Evidence Against Specific Nucleation SitesJournal of Molecular Biology, 2003
- Contact order dependent protein folding rates: Kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferencesProteins-Structure Function and Bioinformatics, 2003
- Hammond Behavior versus Ground State Effects in Protein Folding: Evidence for Narrow Free Energy Barriers and Residual Structure in Unfolded StatesJournal of Molecular Biology, 2003
- Fast and Slow Intermediate Accumulation and the Initial Barrier Mechanism in Protein FoldingJournal of Molecular Biology, 2002
- Protein Folding Kinetics Beyond the Φ Value: Using Multiple Amino Acid Substitutions to Investigate the Structure of the SH3 Domain Folding Transition StateJournal of Molecular Biology, 2002
- The single helix in protein L is largely disrupted at the rate-limiting step in foldingJournal of Molecular Biology, 1998
- The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for foldingJournal of Molecular Biology, 1998
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Characterization of the critical state in protein foldingJournal of Molecular Biology, 1989