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The Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure<sup>*</sup>
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1967
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Protein AssemblyStructural BioinformaticsAltmetric Attention ScoreMolecular BiologyBiochemistry 1967Protein FoldingProtein X-ray CrystallographyBiophysicsProtein ChemistryBiochemistryBiomolecular AnalysisConformational StudySocial Media PresenceMacromolecular ArchitectureMolecular ModelingBiomolecular ScienceStructural BiologyConformational TransitionsNatural SciencesMolecular BiophysicsMedicine
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure*Betty Davidson and Gerald D. FasmanCite this: Biochemistry 1967, 6, 6, 1616–1629Publication Date (Print):June 1, 1967Publication History Published online1 May 2002Published inissue 1 June 1967https://pubs.acs.org/doi/10.1021/bi00858a008https://doi.org/10.1021/bi00858a008research-articleACS PublicationsRequest reuse permissionsArticle Views1584Altmetric-Citations241LEARN 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-Alertsclose Get e-Alerts
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