Predicting protein folding cores by empirical potential functions
- 1 March 2009
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 483 (1), 16-22
- https://doi.org/10.1016/j.abb.2008.12.011
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- The Folding Pathway of T4 Lysozyme: The High-resolution Structure and Folding of a Hidden IntermediateJournal of Molecular Biology, 2007
- The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure‐folding transition stateProtein Science, 2006
- Localized Nature of the Transition-state Structure in Goat α-Lactalbumin FoldingJournal of Molecular Biology, 2004
- Predicting Changes in the Stability of Proteins and Protein Complexes: A Study of More Than 1000 MutationsJournal of Molecular Biology, 2002
- Topological and energetic factors: what determines the structural details of the transition state ensemble and “en-route” intermediates for protein folding? an investigation for small globular proteinsJournal of Molecular Biology, 2000
- Defining Protein Ensembles with Native-state NH Exchange: Kinetics of Interconversion and Cooperative Units from Combined NMR and MS AnalysisJournal of Molecular Biology, 1999
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Amide hydrogen exchange and internal dynamics the chemotactic protein CheY from Escherichia coliJournal of Molecular Biology, 1997
- How does a protein fold?Nature, 1994
- A Correlation of Reaction RatesJournal of the American Chemical Society, 1955