Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme

Computation of the spectroscopic effects expected in a protein with independent pressure-denaturable domains shows that an apparent one-step change will be observed in all but extreme cases and that the volume changes calculated from the experimental data can grossly underestimate the change in volume upon denaturation of the whole protein.

Abstract

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPlurality of pressure-denatured forms in chymotrypsinogen and lysozymeThomas M. Li, John W. Hook, III, Harry G. Drickamer, and Gregorio WeberCite this: Biochemistry 1976, 15, 25, 5571–5580Publication Date (Print):December 1, 1976Publication History Published online1 May 2002Published inissue 1 December 1976https://pubs.acs.org/doi/10.1021/bi00670a023https://doi.org/10.1021/bi00670a023research-articleACS PublicationsRequest reuse permissionsArticle Views165Altmetric-Citations119LEARN 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