Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins
- 28 July 2000
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 300 (5), 1335-1359
- https://doi.org/10.1006/jmbi.2000.3901
Abstract
No abstract availableKeywords
This publication has 83 references indexed in Scilit:
- Role of main-chain electrostatics, hydrophobic effect and side-chain conformational entropy in determining the secondary structure of proteinsJournal of Molecular Biology, 1998
- Prediction of the three-dimensional structure of proteins using the electrostatic screening model and hierarchic condensationProteins-Structure Function and Bioinformatics, 1998
- Accurate ab Initio Quantum Chemical Determination of the Relative Energetics of Peptide Conformations and Assessment of Empirical Force FieldsJournal of the American Chemical Society, 1997
- Determination of the conformation of folding initiation sites in proteins by computer simulationProteins-Structure Function and Bioinformatics, 1995
- Role of Electrostatic Screening in Determining Protein Main Chain Conformational PreferencesBiochemistry, 1995
- Hydrogen bond strength and β‐sheet propensities: The role of a side chain blocking effectProteins-Structure Function and Bioinformatics, 1994
- Primary structure effects on peptide group hydrogen exchangeProteins-Structure Function and Bioinformatics, 1993
- Use of a potential of mean force to analyze free energy contributions in protein foldingBiochemistry, 1992
- Molecular dynamics study of the structure and dynamics of a protein molecule in a crystalline ionic environment, Streptomyces griseus protease ABiochemistry, 1990
- Microfolding: Conformational probability map for the alanine dipeptide in water from molecular dynamics simulationsProteins-Structure Function and Bioinformatics, 1988