Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTConformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsPeter Y. Chou and Gerald D. FasmanCite this: Biochemistry 1974, 13, 2, 211–222Publication Date (Print):January 15, 1974Publication History Published online1 May 2002Published inissue 15 January 1974https://pubs.acs.org/doi/10.1021/bi00699a001https://doi.org/10.1021/bi00699a001research-articleACS PublicationsRequest reuse permissionsArticle Views4453Altmetric-Citations1718LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail…
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Secondary structure predictions suggest that position 136 lies in an alpha-helix from residues 130 to 150, which includes the receptor-binding domain from 140 to 150.
“Secondary structure predictions (54,55) suggest that position 136 is part of an a-helix that extends between residues 130 and 150 (13,24), encompassing the receptor-binding domain from 140 to 150 (22).”
From Apolipoprotein E2-Christchurch (136 Arg----Ser). New variant of human apolipoprotein E in a patient with type III hyperlipoproteinemia. (1987) · cites this paper as [54]
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- Authors
- Chou, P. Y., & Fasman, G. D.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1974-01-15
- Volume
- 13
- Issue
- 2
- Pages
- 211-222
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1963550288
- Cited by
- 2,172
- References
- 0
- Citations by year
- 2026: 14 · 2025: 16 · 2024: 19 · 2023: 10 · 2022: 19 · 2021: 25 · 2020: 24 · 2019: 40 · 2018: 36 · 2017: 34 · 2016: 35 · 2015: 37 · 2014: 35 · 2013: 35 · 2012: 44
- FWCI
- 30.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- helix-coil transition, helical regions, protein secondary structure
- MeSH terms
- Amino Acid Sequence, Amino Acids, Carboxypeptidases, Chymotrypsin, Cytochrome c Group, Cytochromes, Hemoglobins, Insulin, Mathematics, Molecular Conformation, Muramidase, Muscle Proteins, Myoglobin, Pancreatic Elastase, Papain, Protein Conformation, Protein Denaturation, Proteins, Ribonucleases, Staphylococcus, Subtilisins, X-Ray Diffraction
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