Different circular permutations produced different folding nuclei in proteins: a computational study11Edited by A. R. Fersht
- 1 February 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 306 (1) , 121-132
- https://doi.org/10.1006/jmbi.2000.4375
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Differential stabilization of two hydrophobic cores in the transition state of the villin 14T folding reactionJournal of Molecular Biology, 2000
- β-Sheet Proteins with Nearly Identical Structures Have Different Folding IntermediatesBiochemistry, 2000
- Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.Nature Structural & Molecular Biology, 1999
- Prediction of protein-folding mechanisms from free-energy landscapes derived from native structuresProceedings of the National Academy of Sciences, 1999
- Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavityJournal of Molecular Biology, 1999
- Identification of kinetically hot residues in proteinsProtein Science, 1998
- A metastable state in folding simulations of a protein modelNature Structural & Molecular Biology, 1998
- De Novo Protein Design: Fully Automated Sequence SelectionScience, 1997
- De novo design of the hydrophobic cores of proteinsProtein Science, 1995
- Specific Nucleus as the Transition State for Protein Folding: Evidence from the Lattice ModelBiochemistry, 1994