Micro-environment effect on the structure of synthetic substrates of thermolysin

Letters in Peptide Science

Volumn 4, Issue 4-6, 1997, Pages 391-395

  Baltora Rosset, Sylvie ^a   Marty, Danielle ^a   Dupradeau, François Yves ^a   Pauthe, Emmanuel ^b   Larreta Garde, Véronique ^b   Gacel, Gilles ^a   Monti, Jean Pierre ^a  

^a UNIVERSITÉ DE PICARDIE JULES VERNE   (France)

^b UNIVERSITÉ DE CERGY PONTOISE   (France)

Author keywords

Molecular modeling; NMR; Peptides

Indexed keywords

EID: 0013492989     PISSN: 09295666     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02442905     Document Type: Article

References (24)

1. Endo, S., J. Fermentation Tech., 40 (1962) 346.
2. a. Imanaka, T., Shibazaki, M. and Takagi, M., Nature, 312 (1986) 110.
3. b. Malfroy, B. and Schwartz, J.C., Biochem. Biophys. Res. Commun., 130 (1985) 372.
4. c. Hersh, L.B. and Morihara, K., J. Biol. Chem., 261 (1986) 6433.
5. Dunn, B.M., in Beyond, R.J. and Bond, J.S. (Eds.) Proteolytic Enzymes: A Practical Approach, IRL Press, Oxford, 1989, pp. 57-61.
6. Ligné, T., Pauthe, E., Monti, J.P., Gacel, G. and Larreta-Garde, V., Biochim. Biophys. Acta, 1337 (1997) 143.
7. Pourplanche, C., Lambert, C., Berjot, M., Marx, J., Chopard, C., Alix, A.J.P. and Larreta-Garde, V., J. Biol. Chem., 269 (1994) 31585.
8. a. Weimer, S.J., Kollman, P.A., Case, D.A., Singh, U.C., Ghio, C., Alagona, G., Profeta, Jr., S. and Weimer, P., J. Am. Chem. Soc., 106 (1984) 765.
9. b. Weimer, S.J., Kollman, P.A., Nguyen, D.T. and Case, D.A., J. Comput. Chem., 7 (1986) 230.
10. McDonald, D.Q. and Still, W.C., Tetrahedron Lett., 33 (1992) 7743.
11. McDonald, D.Q. and Still, W.C., Tetrahedron Lett., 33 (1992) 7747.
12. a. Chang, G., Guida, W.C. and Still, W.C., J. Am. Chem. Soc., 111 (1989) 4379.
13. b. Saunders, M., Houk, K.N., Wu, Y.D., Still, W.C., Lipton, M., Chang, G. and Guida, W.C., J. Am. Chem. Soc., 112 (1990) 1419.
14. Brünger, A.T., Clore, G.M., Gronenborn, A.M., Saffrich, R. and Nilges, M., Science, 261 (1993) 328.
15. a. Ohnishi, M. and Urry, D.W., Biochem. Biophys. Res. Comm., 36 (1969) 194.
16. b. Kessler, H., Angew. Chem. Int. Ed. Engl., 21 (1982) 512.
17. Kövèr, K.E., Jiao, D., Fang, S. and Hruby, V.J., J. Org. Chem., 59 (1994) 991.
18. Mierke, D.E., Kurz, M. and Kessler, H., J. Am. Chem. Soc., 116 (1994) 1042.
19. a. Matthews, B.W., Jansonius, J.N. and Colman, P.M., Nature, 238 (1972) 37.
20. b. Colman, P.M., Jansonius, J.N. and Matthews, B.W., J. Mol. Biol., 70 (1972) 701.
21. a. Roderick, S., Fournié-Zaluski, M.C., Roques, B. and Matthews, B.W., Biochemistry, 28 (1989) 1493.
22. b. Izquierdo, M.C. and Ross, L.S., J. Am. Chem. Soc., 112 (1990) 6054.
23. Morgan, B.P., Holland, D.R., Matthews, B.W. and Bartlett, P.A., J. Am. Chem. Soc., 116 (1994) 3251.
24. Holden, H.M., Tronrud, D.E., Monzingo, A.F., Weaver, L.H. and Matthews, B.W., Biochemistry, 26 (1987) 8542.