A Thermodynamic and Kinetic Analysis of the Folding Pathway of an SH3 Domain Entropically Stabilised by a Redesigned Hydrophobic Core
- 18 April 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 328 (1) , 221-233
- https://doi.org/10.1016/s0022-2836(03)00273-0
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Folding of circular permutants with decreased contact order: general trend balanced by protein stability 1 1Edited by A. R. FershtJournal of Molecular Biology, 2001
- Computer-aided design of β-sheet peptides 1 1Edited by J. ThorntonJournal of Molecular Biology, 2001
- Bergerac-SH3: “frustation” induced by stabilizing the folding nucleusJournal of Molecular Biology, 2001
- The SH3-fold Family: Experimental Evidence and Prediction of Variations in the Folding PathwaysJournal of Molecular Biology, 2000
- Stabilisation of α-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase foldingJournal of Molecular Biology, 2000
- The Protein Data BankNucleic Acids Research, 2000
- Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domainJournal 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
- Non-native local interactions in protein folding and stability: introducing a helical tendency in the all β-sheet α-spectrin SH3 domainJournal of Molecular Biology, 1997
- A Correlation of Reaction RatesJournal of the American Chemical Society, 1955