Residue accessibility, hydrogen bonding, and molecular recognition: Metal-chelate probing of active site histidines in chymotrypsins

Biochemistry

Volumn 36, Issue 23, 1997, Pages 6896-6905

  Berna, Patrick P ^a,b   Mrabet, Nadir T ^c   Van Beeumen, Jozef ^d   Devreese, Bart ^d   Porath, Jerker ^b   Vijayalakshmi, Mookambeswaran A ^a  

^a UNIVERSITÉ DE TECHNOLOGIE DE COMPIÈGNE   (France)

^b University of Arizona   (United States)

^c UNIVERSITÉ DE LORRAINE   (France)

^d GHENT UNIVERSITY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN; HISTIDINE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

ANIMALS; BINDING SITES; CATTLE; CHELATING AGENTS; CHROMATOGRAPHY, AFFINITY; CHYMOTRYPSIN; CHYMOTRYPSINOGEN; COPPER; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; HYDROGEN BONDING; IMINO ACIDS; MODELS, MOLECULAR; PROTEIN CONFORMATION; SURFACE PROPERTIES;

BOVINAE;

EID: 0031007424     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9618070     Document Type: Article

References (54)

1. Alard, P. (1991) Ph.D. Dissertation, Université Libre de Bruxelles, Brussels, Belgium.
2. Alard, P., & Wodak, S. J. (1991) J. Comput. Chem. 12, 918-922.
3. Andersson, L., & Sulkowski, E. (1992) J. Chromatogr. 604, 13-17.
4. Arnold, F. (1991) BioTechnology 9, 151-156.
5. Bachovchin, W. W. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7948-7951.
6. Bachovchin, W. W. (1986) Biochemistry 25, 7751-7759.
7. Bartunik, H. D., Summers, L. J., & Bartsch, H. H. (1989) J. Mol. Biol. 210, 813-828.
8. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Jr., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) J. Mol. Biol. 112, 535-542.
9. Blevins, R. A., & Tulinsky, A. (1985) J. Biol. Chem. 260, 4264-4275.
10. Botros, H. G., & Vijayalaksmi, M. (1989) J. Chromatogr. 495, 113-122.
11. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254.
12. Brooks, A., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) J. Comput. Chem. 4, 187-217.
13. Connolly, M. L. (1983) Science 221, 709-713.
14. Corradini, D., El Rassi, Z., Horvath, C., Guerra, G., & Horne, W. (1988). J. Chromatogr. 458, 1-11.
15. Cruickshank, W. H., & Kaplan, H. (1975) Biochem. J. 147, 411-416.
16. Delhaise, P., Bardiaux, M., & Wodak, S. J. (1984) J. Mol. Graphics 2, 103-106.
17. Derewenda, Z. S., Derewenda, U., & Kobos, P. M. J. (1994) J. Mol. Biol. 241, 83-93.
18. Dixon, M. M., & Matthews, B. W. (1989) Biochemistry 28, 7033-7038.
19. Dreyer, W. J., & Neurath, H. (1955) J. Biol. Chem. 217, 527-534.
20. Fahrney, D. E., & Gold, A. M. (1963) J. Am. Chem. Soc. 85, 997-1000.
21. Fazakerley, S., & Best, D. R. (1965) Anal. Biochem. 12, 290-295.
22. Frey, P. A., Whitt, S. A., & Tobin, J. B. (1994) Science 264, 1927-1930.
23. Harel, M., Su, C. T., Frolow, P., Silman, S., & Sussman, J. L. (1991) Biochemistry 30, 5217-5225.
24. Hemdan, E. S., Zhao, Y. J., Sulkowski, E., & Porath, J. (1989) Proc. Natl. Acad Sci. U.S.A. 86, 1811-1815.
25. Hubert, P., & Porath, J. (1981) J. Chromatogr. 206, 164-168.
26. Hummel, B. C. W. (1959) Can. J. Biochem. Physiol. 37, 1393-1399.
27. Hutchens, T. W., & Yip, T. T. (1990) Anal. Biochem. 191, 160-168.
28. Johnson, R. D., Todd, R. J., & Arnold, F. H. (1996) J. Chromatogr. 725, 225-235.
29. Lee, B., & Richards, F. M. (1971) J. Mol. Biol. 55, 379-400.
30. Levitt, M., & Lifson, S. (1969) J. Mol. Biol. 46, 269-279.
31. Liu, Y., & Yu, S. (1990) J. Chromatogr. 515, 169-173.
32. Markley, J. L., & Ibanez, I. B. (1978) Biochemistry 17, 4627-4639.
33. McDonald, I. K., & Thornton, J. M. (1994) Protein Eng. 8, 217-224.
34. Melchior, W. B., & Fahrney, D. (1970) Biochemistry 9, 251-258.
35. Mrabet, N. T. (1992) Biochemistry 31, 2690-2702.
36. Nakagawa, Y., & Bender, M. L. (1970) Biochemistry 9, 259-264.
37. Nakagawa, Y., Yip, T.-T., Belew, M., & Porath, J. (1988) Anal. Biochem. 168, 75-81.
38. Perrin, D. D., & Dempsey, B. (1987) in Buffers far pH and Metal Ion Control, p 57, Chapman & Hall Ltd., London.
39. Porath, J., Carlsson, J., Olsson, I., & Belfrage, G. (1975) Nature 258, 598-599.
40. Reynolds, W. F., Peat, I. R., Freedman, M. H., & Lyerla, J. R., Jr. (1973) J. Am. Chem. Soc. 95, 328-331.
41. Rovery, M., Poilroux, M., Curnier, A., & Desnuelle, P. (1955) Biochim. Biophys. Acta 17, 565-572.
42. Scatchard, G. (1949) Ann. N.Y. Acad. Sci. 51, 660-672.
43. Schoellmann, G., & Shaw, E. (1963) Biochemistry 2, 252-255.
44. Schwert, G. W., & Takenaka, Y. (1955) Biochim. Biophys. Acta 6, 570-578.
45. Smith, S. O., Farr-Jones, S., Griffin, R. G., & Bachovchin W. W. (1989) Science 244, 961-964.
46. Sulkowski, E. (1985) Trends Biotechnol. 3, 1-7.
47. Sulkowski, E. (1987) in Protein Purification: Micro to Macro (Burgess, R. R., Ed.) pp 149-162, Alan R. Liss Inc., New York, NY.
48. Sulkowski, E. (1989) BioEssays 10, 170-175.
49. Tobin, J. B., Whitt, S. A., Cassidy, C. S., & Frey, P. A. (1995) Biochemistry 34, 6919-6924.
50. Vijayalakshmi, M. A. (1989) Trends Biotechnol. 7, 71-76.
51. Wang, D., Bode, W., & Huber, R. (1985) J. Mol. Biol. 185, 595-624.
52. Wilcox, P. E. (1970) Methods Enzymol. 19, 64-108.
53. Wodak, S. J., van Belle, D., & Prevost, M. (1995) in Computer Modelling in Molecular Biology (Goodfellow, J. M., Ed.) pp 61-102, VCH, Weinheim, Germany.
54. Zhao, Y. J., Sulkowski, E., & Porath, J. (1991) Eur. J. Biochem. 202, 1115-1119.