The influence of short-range interactions on protein conformation. I. Side chain-backbone interactions within a single peptide unit.
- 1 December 1968
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 61 (4) , 1163-1170
- https://doi.org/10.1073/pnas.61.4.1163
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Prediction of alpha-helical regions in proteins of known sequence.Proceedings of the National Academy of Sciences, 1968
- Minimization of polypeptide energy. I. Preliminary structures of bovine pancreatic ribonuclease S-peptide.Proceedings of the National Academy of Sciences, 1967
- Conformational Analysis of Macromolecules. IV. Helical Structures of Poly-L-Alanine, Poly-L-Valine, Poly-β-Methyl-L-Aspartate, Poly-γ-Methyl-L-Glutamate, and Poly-L-TyrosineThe Journal of Chemical Physics, 1967
- Three-dimensional Structure of Tosyl-α-chymotrypsinNature, 1967
- Recognition of α-helical segments in proteins of known primary structureJournal of Molecular Biology, 1967
- Use of Helical Wheels to Represent the Structures of Proteins and to Identify Segments with Helical PotentialBiophysical Journal, 1967
- Tertiary Structure of RibonucleaseNature, 1967
- Correlation between the distribution of amino acids and alpha helicesBiophysical Journal, 1966
- The Influence of Amino Acid Sequence on Protein StructureBiophysical Journal, 1965
- Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å ResolutionNature, 1965