The influence of short-range interactions on protein conformation. I. Side chain-backbone interactions within a single peptide unit.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 61 ·No. 4 ·1968-12-00 ·Pages 1163-70

Kotelchuck D, Scheraga HA

Abstract

暂无摘要

MeSH Terms

Alanine Amino Acid Sequence Arginine Asparagine Aspartic Acid Binding Sites Cystine Glutamates Glutamine Glycine Histidine Isoleucine Kinetics Leucine Lysine Methionine Muramidase/analysis Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine

Chemicals

Glutamates Isoleucine Glutamine Threonine Aspartic Acid Tyrosine Serine Phenylalanine Cystine Histidine Asparagine Tryptophan Arginine Proline Methionine Muramidase Leucine Valine Lysine Alanine Glycine

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Kotelchuck D

Scheraga H A

References (10)

10 references, click to expand

Conformation of analysis of macromolecules. IV. Helical structures of poly-L-alanine, poly-L-valine, poly-beta-methyl-L-aspartate, poly-gamma-methyl-L-glutamate, and poly-L-tyrosine.
J Chem Phys. 1967 Jun 1;46(11):4410-26 PMID: 6043847
Use of helical wheels to represent the structures of proteins and to identify segments with helical potential.
Biophys J. 1967 Mar;7(2):121-35 PMID: 6048867
Three-dimensional structure of tosyl-alpha-chymotrypsin.
Nature. 1967 May 13;214(5089):652-6 PMID: 6049071
Minimization of polypeptide energy. I. Preliminary structures of bovine pancreatic ribonuclease S-peptide.
Proc Natl Acad Sci U S A. 1967 Aug;58(2):420-7 PMID: 5233450
Prediction of alpha-helical regions in proteins of known sequence.
Proc Natl Acad Sci U S A. 1968 Aug;60(4):1519-26 PMID: 5244757
Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.
Nature. 1965 May 22;206(4986):757-61 PMID: 5891407
The influence of amino-acid sequence on protein structure.
Biophys J. 1965 Nov;5(6):809-22 PMID: 5884309
Correlation between the distribution of amino acids and alpha helices.
Biophys J. 1966 May;6(3):367-70 PMID: 5962284
Recognition of alpha-helical segments in proteins of known primary structure.
J Mol Biol. 1967 Mar 14;24(2):313-22 PMID: 6030030
Tertiary structure of ribonuclease.
Nature. 1967 Mar 4;213(5079):862-5 PMID: 6043657

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.61.4.1163

Published

1968-12-00

Pages

1163-70

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC225233

Subset

External Links

PubMed source DOI: 10.1073/pnas.61.4.1163 PMC Full Text View journal details

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The influence of short-range interactions on protein conformation. I. Side chain-backbone interactions within a single peptide unit.

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