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 peptide
- 18 December 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 284 (5) , 1597-1609
- https://doi.org/10.1006/jmbi.1998.2264
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Protein Folding: A Perspective from Theory and ExperimentAngewandte Chemie International Edition in English, 1998
- Insight into a Random Coil Conformation and an Isolated Helix: Structural and Dynamical Characterisation of the C-Helix Peptide from Hen LysozymeJournal of Molecular Biology, 1996
- Toward a Description of the Conformations of Denatured States of Proteins. Comparison of a Random Coil Model with NMR MeasurementsThe Journal of Physical Chemistry, 1996
- 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
- Protein secondary structure predictionCurrent Opinion in Structural Biology, 1995
- Amide Hydrogen Exchange in a Highly Denatured State: Hen Egg-white Lysozyme in UreaJournal of Molecular Biology, 1994
- Folding of peptide fragments comprising the complete sequence of proteinsJournal of Molecular Biology, 1992
- Temperature dependence of the hydrophobic interaction in protein folding.Proceedings of the National Academy of Sciences, 1986
- Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frameJournal of the American Chemical Society, 1984
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977