John A. Schellman

Abstract The stability curve of a protein is defined as the plot of the free energy of unfolding as a function of temperature. For most proteins the change in heat capacity on denaturation, or unfolding, is large but approximately constant. When unfolding is s two‐state process, most of the salient features of the stability curves of proteins can be derived from this fact. A number of relations are obtained, including the special features of low‐temperature denaturation, the properties of the maximum in stability, and the interrelationships of the characteristic temperatures of the protein. The paper closes with a formula that permits one to calculate small changes in stabilization free energy from changes in the melting temperature of the protein.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSymmetry rules for optical rotationJohn A. SchellmanCite this: Acc. Chem. Res. 1968, 1, 5, 144–151Publication Date (Print):May 1, 1968Publication History Published online1 May 2002Published inissue 1 May 1968https://doi.org/10.1021/ar50005a003Request reuse permissionsArticle Views1242Altmetric-Citations350LEARN 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 InReddit PDF (881 KB) Get e-Alertsclose Get e-Alerts

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTCircular dichroism and optical rotationJohn A. SchellmanCite this: Chem. Rev. 1975, 75, 3, 323–331Publication Date (Print):June 1, 1975Publication History Published online1 May 2002Published inissue 1 June 1975https://pubs.acs.org/doi/10.1021/cr60295a004https://doi.org/10.1021/cr60295a004research-articleACS PublicationsRequest reuse permissionsArticle Views3584Altmetric-Citations301LEARN 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

Abstract Solvent denaturation is developed along thermodynamic lines rather than from multiple‐binding theory. Almost all the relations derivable from site‐binding theory have their counterparts in the thermodynamic formulation showing that the details of binding models may be sufficient but are not necessary for the general description of solvent denaturation. Equations are derived for the effect of denaturant concentration on stability at constant temperature and on t m . It is recommended that the thermodynamic treatment be used instead of binding models unless stoichiometric interactions are demonstrable experimentally.