Position dependence of non-polar amino acid intrinsic helical propensities
- 24 April 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 278 (1) , 279-289
- https://doi.org/10.1006/jmbi.1998.1682
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- N‐ and C‐capping preferences for all 20 amino acids in α‐helical peptidesProtein Science, 1995
- The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assembliesJournal of Computational Chemistry, 1995
- α‐Helix‐forming propensities in peptides and proteinsProteins-Structure Function and Bioinformatics, 1994
- Rules for α-Helix Termination by GlycineScience, 1994
- Biased Probability Monte Carlo Conformational Searches and Electrostatic Calculations for Peptides and ProteinsJournal of Molecular Biology, 1994
- Large differences in the helix propensities of alanine and glycineNature, 1991
- Physical reasons for secondary structure stability: α‐Helices in short peptidesProteins-Structure Function and Bioinformatics, 1991
- Side chain–backbone hydrogen bonding contributes to helix stability in peptides derived from an α‐helical region of carboxypeptidase AProteins-Structure Function and Bioinformatics, 1991
- Calculation of protein extinction coefficients from amino acid sequence dataAnalytical Biochemistry, 1989
- Determination of the helix and β form of proteins in aqueous solution by circular dichroismBiochemistry, 1974