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Structural Chemistry of Peptides Containing Backbone Expanded Amino Acid Residues: Conformational Features of β, γ, and Hybrid Peptides
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTStructural Chemistry of Peptides Containing Backbone Expanded Amino Acid Residues: Conformational Features of β, γ, and Hybrid PeptidesPrema. G. Vasudev†, Sunanda Chatterjee‡, Narayanaswamy Shamala*†, and Padmanabhan Balaram*‡View Author Information Department of Physics and Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India* To whom correspondence should be addressed. Fax: (+91) 80-2360-2602. E-mail: [email protected]. Fax: (+91) 80-2360-0535. E-mail: [email protected]†Department of Physics.‡Molecular Biophysics Unit.Cite this: Chem. Rev. 2011, 111, 2, 657–687Publication Date (Web):September 15, 2010Publication History Received25 March 2010Published online15 September 2010Published inissue 9 February 2011https://pubs.acs.org/doi/10.1021/cr100100xhttps://doi.org/10.1021/cr100100xreview-articleACS PublicationsCopyright © 2010 American Chemical SocietyRequest reuse permissionsArticle Views6351Altmetric-Citations295LEARN 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 Other access optionsGet e-AlertscloseSupporting Info (2)»Supporting Information Supporting Information SUBJECTS:Conformation,Hydrogen,Monomers,Noncovalent interactions,Peptides and proteins Get e-Alerts
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Self-citationHelical conformations in a polyamide of the nylon-3 family
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Self-citationBiophysical and Structural Characterization of a Robust Octameric β-Peptide Bundle
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Self-citationFirst Observation of Two Consecutive γ Turns in a Crystalline Linear Dipeptide
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Self-citationPoly-β-L-aspartic Acid. Synthesis through Pentachlorophenyl Active Ester and Conformational Studies
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Self-citationIsomerization of the Xaa-Pro peptide bond induced by ionic interactions of arginine
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Metadata
- Authors
- Vasudev, P. G., Chatterjee, S., Shamala, N., & Balaram, P.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-09-15
- Volume
- 111
- Issue
- 2
- Pages
- 657-687
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1988531810
- Cited by
- 329
- References
- 156
- FWCI
- 1.96
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.