Exploring the Folding Funnel of a Polypeptide Chain by Biophysical Studies on Protein Fragments
- 22 January 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 285 (3) , 1309-1333
- https://doi.org/10.1006/jmbi.1998.2249
Abstract
No abstract availableKeywords
This publication has 74 references indexed in Scilit:
- 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, 1997
- Detection of residue contacts in a protein folding intermediateProceedings of the National Academy of Sciences, 1997
- A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein FoldingJournal of Molecular Biology, 1995
- Acid and Thermal Denaturation of Barnase Investigated by Molecular Dynamics SimulationsJournal of Molecular Biology, 1995
- Funnels, pathways, and the energy landscape of protein folding: A synthesisProteins-Structure Function and Bioinformatics, 1995
- Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state.Proceedings of the National Academy of Sciences, 1994
- Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopyBiochemistry, 1991
- Sequential assignment of the proton nuclear magnetic resonance spectrum of barnaseBiochemistry, 1990
- Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frameJournal of the American Chemical Society, 1984
- Coherence transfer by isotropic mixing: Application to proton correlation spectroscopyJournal of Magnetic Resonance (1969), 1983