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• W2113360613 abstract "FEBS LettersVolume 41, Issue 2 p. 211-215 Full-length articleFree Access A microcalorimetric study on the unfolding of E. coli ribosome Kin-Ping Wong, Corresponding Author Kin-Ping Wong Department of Chemistry, University of South Florida Tampa, Florida 33620, USAPublic Health Service Research Career Development Awardee (GM 70628), to whom all correspondence should be addressed.Search for more papers by this authorJohn M. Dunn, John M. Dunn Department of Chemistry, University of South Florida Tampa, Florida 33620, USASearch for more papers by this authorJesse S. Binford, Jesse S. Binford Department of Chemistry, University of South Florida Tampa, Florida 33620, USASearch for more papers by this author Kin-Ping Wong, Corresponding Author Kin-Ping Wong Department of Chemistry, University of South Florida Tampa, Florida 33620, USAPublic Health Service Research Career Development Awardee (GM 70628), to whom all correspondence should be addressed.Search for more papers by this authorJohn M. Dunn, John M. Dunn Department of Chemistry, University of South Florida Tampa, Florida 33620, USASearch for more papers by this authorJesse S. Binford, Jesse S. Binford Department of Chemistry, University of South Florida Tampa, Florida 33620, USASearch for more papers by this author First published: May 01, 1974 https://doi.org/10.1016/0014-5793(74)81214-7Citations: 6AboutPDF 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 onFacebookTwitterLinkedInRedditWechat References 1 M. Nomura, Science, 179, (1973), 864– 873. 2 A.S. Spirin, N.A. Kisselev, R.S. Shukulov, A.A. Bogdanov, Biokhimya, 28, (1963), 920– 930. 3 K.A. Cammack, H.E. Wade, Biochem. J., 96, (1965), 671– 680. 4 R.F. Gesteland, J. Mol. Biol., 18, (1966), 356– 371. 5 L.P. Gavrilova, D.A. Ivanov, A.S. Spirin, J. Mol. Biol., 16, (1966), 473– 489. 6 M. Tal, Biochim. Biophys. Acta, 195, (1969), 76– 86. 7 P. Traub, S. Mizushima, C.U. Lowry, M. Nomura, Meth. Enzymol., 20, (1971), 391– 407. 8 J.M. Sturtevant, P.A. Lyons, J. Chem. Thermodynamics, 1, (1969), 201– 209. 9 S.F. Velick, J.P. Baggot, J.M. Sturtevant, Biochemistry, 10, (1971), 779– 786. 10 G. Anderegg, Helv. Chim. Acta, 47, (1963), 1801– 1814. 11 J.J. Christensen, R.M. Izaxi, D.D. Wrathall, L.D. Hansen, J. Chem. Soc. A, (1969), 1212– 1223. 12 M. Woodhead, M. Paabo, R.A. Robinson, R.G. Bates, J. Research Nat'l. Bur. Std., 69A, (1965), 263– 270. 13 A.S. Spirin, Prog. Biophys. Mol. Biol., 19, (1969), 135– 174. 14 P. Traub, M. Nomura, J. Mol. Biol., 40, (1969), 391– 413. 15 J.T. Edsall, J. Am. Chem. Soc., 57, (1935), 1506– 1507. 16 R.L. Bohon, W.F. Claussen, J. Am. Chem. Soc., 73, (1951), 1571– 1578. 17 C. Tanford, Adv. Prot. Chem., 23, (1968), 121– 282. Citing Literature Volume41, Issue2May 01, 1974Pages 211-215 ReferencesRelatedInformation" @default.
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