Rules for Antiparallel β-Sheet Design: <scp>d</scp>-Pro-Gly Is Superior to <scp>l</scp>-Asn-Gly for β-Hairpin Nucleation¹

Abstract

ADVERTISEMENT RETURN TO ISSUEPREVCommunicationNEXTRules for Antiparallel β-Sheet Design: d-Pro-Gly Is Superior to l-Asn-Gly for β-Hairpin Nucleation1Heather E. Stanger and Samuel H. GellmanView Author Information Department of Chemistry, University of Wisconsin Madison, Wisconsin 53706 Cite this: J. Am. Chem. Soc. 1998, 120, 17, 4236–4237Publication Date (Web):April 22, 1998Publication History Received27 October 1997Published online22 April 1998Published inissue 1 May 1998https://pubs.acs.org/doi/10.1021/ja973704qhttps://doi.org/10.1021/ja973704qrapid-communicationACS PublicationsCopyright © 1998 American Chemical SocietyRequest reuse permissionsArticle Views1685Altmetric-Citations236LEARN 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 (1)»Supporting Information Supporting Information SUBJECTS:Conformation,Peptides and proteins,Protein folding,Sodium,Solution chemistry Get e-Alerts