Characterization of the Folding Energy Landscapes of Computer Generated Proteins Suggests High Folding Free Energy Barriers and Cooperativity may be Consequences of Natural Selection
- 13 March 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 338 (3) , 573-583
- https://doi.org/10.1016/j.jmb.2004.02.055
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Simple two-state protein folding kinetics requires near-levinthal thermodynamic cooperativityProteins-Structure Function and Bioinformatics, 2003
- Solvation Effects and Driving Forces for Protein Thermodynamic and Kinetic Cooperativity: How Adequate is Native-centric Topological Modeling?Journal of Molecular Biology, 2003
- Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: how applicable is the transition state picture to folding and unfolding?Journal of Molecular Biology, 2002
- Lack of definable nucleation sites in the rate-limiting transition state of barnase under native conditions 1 1Edited by C. R. MatthewsJournal of Molecular Biology, 2002
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Bayesian statistical analysis of protein side‐chain rotamer preferencesProtein Science, 1997
- Kinetics of Folding of the IgG Binding Domain of Peptostreptoccocal Protein LBiochemistry, 1997
- Evidence for a Two-State Transition in the Folding Process of the Activation Domain of Human Procarboxypeptidase A2Biochemistry, 1995
- The nature of the initial step in the conformational folding of disulphide-intact ribonuclease ANature Structural & Molecular Biology, 1995
- Principles of protein folding — A perspective from simple exact modelsProtein Science, 1995