Dissecting the stability of a β-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the β-turn and β-strand contributions to folding 1 1Edited by P. E. Wright
- 1 October 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 292 (5), 1051-1069
- https://doi.org/10.1006/jmbi.1999.3119
Abstract
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This publication has 96 references indexed in Scilit:
- Modulation of intrinsic φ,ψ propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a β-hairpin peptideJournal of Molecular Biology, 1998
- Sequence requirements for stabilization of a peptide reverse turn in water solutionEuropean Journal of Biochemistry, 1998
- Solution Structure of α2D, a Nativelike de Novo Designed ProteinJournal of the American Chemical Society, 1998
- Role of β-turn residues in β-hairpin formation and stability in designed peptidesJournal of Molecular Biology, 1997
- Torsion angle dynamics for NMR structure calculation with the new program DyanaJournal of Molecular Biology, 1997
- Comparison between the φ Distribution of the Amino Acids in the Protein Database and NMR Data Indicates that Amino Acids have Various φ Propensities in the Random Coil ConformationJournal of Molecular Biology, 1995
- Elucidating the Folding Problem of Helical Peptides using Empirical Parameters. II†. Helix Macrodipole Effects and Rational Modification of the Helical Content of Natural PeptidesJournal of Molecular Biology, 1995
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Conformation of twisted β-pleated sheets in proteinsJournal of Molecular Biology, 1973