Title: Hydrophobic interaction in thermolysin specificity
Abstract: FEBS LettersVolume 142, Issue 2 p. 297-300 Full-length articleFree Access Hydrophobic interaction in thermolysin specificity M. Pank, M. Pank Institute of Chemistry, Estonian Academy of Sciences, Estonian Academy of Sciences, PO Box 670, Tallinn 200026, USSRSearch for more papers by this authorO. Kirret, O. Kirret Institute of Chemistry, Estonian Academy of Sciences, Estonian Academy of Sciences, PO Box 670, Tallinn 200026, USSRSearch for more papers by this authorN. Paberit, N. Paberit Institute of Chemical Physics and Biophysics, Estonian Academy of Sciences, PO Box 670, Tallinn 200026, USSRSearch for more papers by this authorA. Aaviksaar, A. Aaviksaar Institute of Chemical Physics and Biophysics, Estonian Academy of Sciences, PO Box 670, Tallinn 200026, USSRSearch for more papers by this author M. Pank, M. Pank Institute of Chemistry, Estonian Academy of Sciences, Estonian Academy of Sciences, PO Box 670, Tallinn 200026, USSRSearch for more papers by this authorO. Kirret, O. Kirret Institute of Chemistry, Estonian Academy of Sciences, Estonian Academy of Sciences, PO Box 670, Tallinn 200026, USSRSearch for more papers by this authorN. Paberit, N. Paberit Institute of Chemical Physics and Biophysics, Estonian Academy of Sciences, PO Box 670, Tallinn 200026, USSRSearch for more papers by this authorA. Aaviksaar, A. Aaviksaar Institute of Chemical Physics and Biophysics, Estonian Academy of Sciences, PO Box 670, Tallinn 200026, USSRSearch for more papers by this author First published: June 07, 1982 https://doi.org/10.1016/0014-5793(82)80156-7Citations: 11 To whom correspondence should be addressed AboutPDF 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 References 1 H. Matsubara, R. Sasaki, A. Singer, T.H. Jukes, Arch. Biochem. Biophys., 115, (1965), 324– 331. 2 K. Morihara, H. Tsuzuki, Eur. J. Biochem., 15, (1970), 374– 380. 3 J. Feder, J.M. Schuck, Biochemistry, 9, (1970), 2784– 2791. 4 P.M. Colman, J.N. Jansonius, B.W. Matthews, J. Mol. Biol., 70, (1972), 701– 724. 5 W.L. Bigbee, F.W. Dahlquist, Biochemistry, 13, (1974), 3542– 3549. 6 W.L. Bigbee, F.W. Dahlquist, Biochemistry, 16, (1977), 3798– 3803. 7 W.R. Kester, B.W. Matthews, Biochemistry, 16, (1977), 2506– 2516. 8 J. Murphy, R. Rowlett, S.B. Smith, J. Hoeferlin, Arch. Biochem. Biophys., 202, (1980), 405– 413. 9 M. Pank, O. Kirret, Izv. Akad. Nauk Est. SSR, 28, (1979), 297– 300. 10 S.M. Khan, D.W. Darnall, Anal. Biochem., 86, (1978), 332– 336. 11 T. Fujita, J. Iwasa, C. Hansch, J. Am. Chem. Soc., 86, (1964), 5175– 5180. 12 P.F. Sikk, A.A. Abduvakhabov, A.A. Aaviksaar, Org. React., 12, (1975), 421– 433. 13 A. Leo, C. Hansch, D. Elkins, Chem. Rev., 71, (1971), 525– 616. 14 I.V. Berezin, N.F. Kazanskaya, A.A. Klyosov, K. Martinek, FEBS Lett., 15, (1971), 125– 128. 15 A.A. Aaviksaar, J. Paris, V. Palm, Org. React., 8, (1971), 817– 830. 16 J. Järv, T. Kesvatera, A. Aaviksaar, Eur. J. Biochem., 67, (1976), 315– 322. 17 A.A. Klyosov, B.L. Vallee, Bioorg. Khim., 3, (1977), 806– 815. 18 G. Morgan, J.S. Fruton, Biochemistry, 17, (1978), 3562– 3568. 19 J. Feder, Biochemistry, 6, (1967), 2088– 2093. 20 M.E. Bayliss, S.H. Wilkes, J.M. Prescott, Arch. Biochem. Biophys., 204, (1980), 214– 219. Citing Literature Volume142, Issue2June 07, 1982Pages 297-300 ReferencesRelatedInformation