Aqueous Trifluoroethanol Research Articles

ChemInform Abstract: THE NUCLEOPHILICITY OF AQUEOUS TRIFLUOROETHANOL

Chemischer InformationsdienstVolume 5, Issue 21 Preparative Organic Chemistry ChemInform Abstract: THE NUCLEOPHILICITY OF AQUEOUS TRIFLUOROETHANOL D. J. RABER, D. J. RABERSearch for more papers by this authorM. D. DUKES, M. D. DUKESSearch for more papers by this authorJ. GREGORY, J. GREGORYSearch for more papers by this author D. J. RABER, D. J. RABERSearch for more papers by this authorM. D. DUKES, M. D. DUKESSearch for more papers by this authorJ. GREGORY, J. GREGORYSearch for more papers by this author First published: May 28, 1974 https://doi.org/10.1002/chin.197421143Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinked InRedditWechat No abstract is available for this article. Volume5, Issue21May 28, 1974 RelatedInformation

Vinylic cations from solvolysis. XVII. Unusual solvent effect and common ion rate depression in aqueous trifluoroethanol

Vinylic cations from solvolysis. XVII. Unusual solvent effect and common ion rate depression in aqueous trifluoroethanol

Circular dichroism and viscometric studies on a basic protein from pig brain.

Abstract— A highly purified basic protein prepared from pig brain was studied by circular dichroism and viscometry. The circular dichroism spectrum of the protein in 50% (v/v) aqueous n‐propanol showed two negative bands (at 217‐220 nm and 204 nm); the spectrum in 90% (v/v) aqueous trifluoroethanol similarly showed two negative bands (at 217 nm and at 206 nm). The molar ellipticity of this protein in aqueous solvents was relatively flat and no negative bands were observed above 200 nm. The ηap C of the protein from pig brain was 0‐12 as C → O in tris buffer (0‐1 M, pH 7‐8). On the basis of these studies we concluded that the protein is asymmetric and extended in aqueous systems and contains a maximum of 20 per cent α‐helix in trifluoroethanol.