Reverse turns in blocked dipeptides are intrinsically unstable in water
- 5 December 1990
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 216 (3), 783-796
- https://doi.org/10.1016/0022-2836(90)90399-7
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- Microfolding: Conformational probability map for the alanine dipeptide in water from molecular dynamics simulationsProteins-Structure Function and Bioinformatics, 1988
- Configurational entropy of native proteinsBiophysical Journal, 1987
- Models of thioredoxin hairpin structures: Conformational properties of β‐turn containing sequencesPeptide Science, 1986
- Configuration entropy of the alanine dipeptide in vacuum and in solution: a molecular dynamics studyJournal of the American Chemical Society, 1985
- Comparison of simple potential functions for simulating liquid waterThe Journal of Chemical Physics, 1983
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- β-turns in proteinsJournal of Molecular Biology, 1977
- IUPAC-IUB Commission on Biochemical Nomenclature: Abbreviations and symbols for the description of the conformation of polypeptide chainsJournal of Molecular Biology, 1970