Similarities between the spectrin SH3 domain denatured state and its folding transition state
- 14 April 2000
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 297 (5), 1217-1229
- https://doi.org/10.1006/jmbi.2000.3618
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- 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
- Acceleration of the folding of acylphosphatase by stabilization of local secondary structure.Nature Structural & Molecular Biology, 1999
- Matching theory and experiment in protein foldingCurrent Opinion in Structural Biology, 1999
- High populations of non-native structures in the denatured state are compatible with the formation of the native folded stateJournal of Molecular Biology, 1998
- Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: Description of the folding pathwayProceedings of the National Academy of Sciences of the United States of America, 1997
- 1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure.Journal of Biomolecular NMR, 1997
- Conformational Pathway of the Polypeptide Chain of Chymotrypsin Inhibitor-2 Growing from its N Terminusin vitro. Parallels with the Protein Folding PathwayJournal of Molecular Biology, 1995
- Protein Folding: An unfolding storyCurrent Biology, 1995
- Funnels, pathways, and the energy landscape of protein folding: A synthesisProteins-Structure Function and Bioinformatics, 1995