Assignment and analysis of fluorine nuclear magnetic resonance spectra of 4-fluorotryptophan myoglobins and hemoglobins

Biochemistry

Volumn 36, Issue 12, 1997, Pages 3590-3599

  Pearson, John G ^a   Montez, Bernard ^a   Le, Hongbiao ^a   Oldfield, Eric ^a   Chien, Ellen Y T ^a   Sligar, Stephen G ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN;

ARTICLE; BINDING AFFINITY; CALCULATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ANIMALS; ELECTROSTATICS; HEMOGLOBINS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MYOGLOBIN; PLASMIDS; TRYPTOPHAN; WHALES;

EID: 0030989058     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961664h     Document Type: Article

References (58)

1. Abadan, Y., Chien, E. Y. T., Chu, K., Eng, C. D., Nienhaus, G. U., & Sligar, S. G. (1995) Biophys. J. 68, 2497-2504.
2. Abola, E., Bernstein, F. C., Bryant, S. H., Koetzle, T. F., & Weng, J. (1987) Protein Data Bank, in Crystallographic Databases - Information Content, Software Systems, Scientific Applications (Allen, F. H., Bergerhoff, G., & Sievers, R., Eds.) p 107, Data Commission of the International Union of Crystallography, Bonn, Cambridge, and Chester.
3. Arnone, A., & Silva, M. M. (1992) J. Biol. Chem. 267, 17248-17256.
4. Augspuraer, J. D., & Dykstra, C. E. (1991) J. Phys. Chem. 95, 9230-9238.
5. Augspurger, J. D., Dykstra, C. E., & Oldfield, E. (1991) J. Am. Chem. Soc. 113, 2447-2451.
6. Augspurger, J. D., Pearson, J., Oldfield, E., Dykstra, C. E., Park, K. D., & Schwartz, D. (1992) J. Magn. Reson. 100, 342-357.
7. Batchelor, J. G. (1975) J. Am. Chem. Soc. 97, 3410-3415.
8. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, J. E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) J. Mol. Biol. 112, 535-542.
9. Bode, R., Kunze, G., & Birnbaum, D. (1985) Biochem. Physiol. Pflanzen. 180, 613-619.
10. Bode, R., Schauer, F., & Birnbaum, D. (1986) Biochem. Physiol. Pflanzen. 181, 39-46.
11. Browne, D. T., & Otvos, J. D. (1976) Biochem. Biophys. Res. Commun. 68, 907-913.
12. Bucci, E., & Fronticelli, C. (1965) J. Biol. Chem. 240, PC55.
13. Buckingham, A. D. (1960) Can. J. Chem. 38, 300-307.
14. Buckingham, A. D., & Lawley, K. P. (1960) Mol. Phys. 3, 219-222.
15. Busch, M. R., Mace, J. E., Ho, N. T., & Ho, C. (1991) Biochemistry 30, 1863-1877.
16. Case, D. A., Dyson, H. J., & Wright, P. E. (1994) Methods Enzymol. 239, 392-416.
17. Chaiken, I. M., Freedman, M. H., Lyerla, J. R. J., & Cohen, J. S. (1973) J. Biol. Chem. 248, 884-891.
18. Chiu, M. L. (1986) Ph.D. Dissertation, University of Illinois at Urbana-Champaign, Urbana, IL.
19. de Dios, A. C., & Oldfield, E. (1994) J. Am. Chem. Soc. 116, 5307-5314.
20. de Dios, A. C., Pearson, J. G., & Oldfield, E. (1993) Science 260, 1491-1496.
21. Falke, J. J., Luck, L. A., & Scherrer, J. (1992) Biophys. J. 62, 82-86.
22. Fermi, G., Perutz, M. F., Shaanan, B., & Fourme, R. (1984) J. Mol. Biol. 175, 159-174.
23. Gamcsik, M. P., & Gerig, J. T. (1986) FEBS Lett. 196, 71-74.
24. Gamcsik, M. P., Gerig, J. T., & Swenson, R. B. (1986) Biochim. Biophys. Acta 874, 372-374.
25. Gamcsik, M. P., Gerig, J. T., & Gregory, D. H. (1987) Biochim. Biophys. Acta 912, 303-316.
26. Geris, J. T., Klinkenborg, J. C., & Nieman, R. A. (1983) Biochemistry 22, 2076-2087.
27. Hernan, R. A., & Sligar, S. G. (1995) J. Biol. Chem. 270, 26257-26264.
28. Hernan, R. A., Hui, H. L., Andracki, M. E., Noble, R. W., Sligar, S. G., Walder, J. A., & Walder, R. Y. (1992) Biochemistry 31, 8619-8628.
29. Ho, C., Pratt, E. A., & Rule, G. S. (1989) Biochim. Biophys. Acta 988, 173-184.
30. Hull, W. E., & Sykes, B. D. (1975) J. Mol. Biol. 98, 121-153.
31. Hull, W. E., & Sykes, B. D. (1976) Biochemistry 15, 1535-1546.
32. Imai, K. (1981) Methods Enzymol. 76, 438-449.
33. Kilmartin, J. V., Breen, J. J., Roberts, G. C. K., & Ho, C. (1973) Proc. Natl. Acad. Sci. U.S.A. 70, 1246-1249.
34. Kimber, B. J., Griffiths, D. V., Birdsall, B., King, R. W., Scudder, P., Feeney, J., Roberts, G. C. K., & Burgen, A. S. V. (1977) Biochemistry 16, 3492-3500.
35. Kimber, B. J., Feeney, J., Roberts, G. C. K., Birdsall, B., Griffiths, D. V., & Burgen, A. S. V. (1978) Nature 271, 184-185.
36. Kunze, G., Bode, R., Rintala, H., & Hofemeister, J. (1989) Curr. Genet. 15, 91-98.
37. Kuriyan, J., Wilz, S., Karplus, M., & Petsko, G. A. (1986) J. Mol. Biol. 192, 133-154.
38. Lee, F. S., & Warshel, A. (1992) J. Chem. Phys. 97, 3100-3107.
39. Lian, C., Le, H., Montez, B., Patterson, J., Harrell, S., Laws, D., Matsumura, I., Pearson, J., & Oldfield, E. (1994) Biochemistry 33, 5238-5245.
40. Luck, L. A., & Falke, J. J. (1991a) Biochemistry 30, 6484-6490.
41. Luck, L. A., & Falke, J. J. (1991b) Biochemistry 30, 4248-4256.
42. Luck, L. A., & Falke, J. J. (1991c) Biochemistry 30, 4257-4261.
43. Morris, A. L., MacArthur, M. W., Hutchinson, E. G., & Thornton, J. M. (1992) Proteins 12, 345-364.
44. Pearson, J. G., Oldfield, E., Lee, F. S., & Warshel, A. (1993) J. Am. Chem. Soc. 115, 6851-6862.
45. Peersen, O. B., Pratt, E. A., Truong, H.-T. N., Ho, C., & Rule, G. S. (1990) Biochemistry 29, 3256-3262.
46. Phillips, G. N., Jr., Arduini, R. M., Springer, B. A., & Sligar, S. G. (1990) Proteins: Struct., Funct., Genet. 7, 358-365.
47. Phillips, S. E. V., & Schoenborn, B. P. (1981) Nature 292, 81-82.
48. Pratt, E. A., & Ho, C. (1975) Biochemistry 14, 3035-3040.
49. Robertson, D. E., Kroon, P. A., & Ho, C. (1977) Biochemistry 16, 1443-1451.
50. Rohlfs, R. J., Mathews, A. J., Carver, T. E., Olson, J. S., Springer, B. A., Egeberg, K. D., & Sligar, S. G. (1990) J. Biol. Chem. 265, 3168-3176.
51. Shaanan, B. (1983) J. Mol. Biol. 171, 31-59.
52. Silva, M. M., Rogers, P. H., & Arnone, A. (1992) J. Biol. Chem. 267, 17248-17256.
53. Smith, L. J., Redfield, C., Smith, R. A. G., Dobson, C. M., Clore, G. M., Gronenborn, A. M., Walter, M. R., Naganbushan, T. L., & Wlodawer, A. (1994) Nat. Struct. Biol. 1, 301-310.
54. Springer, B. A., & Sligar, S. G. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 8961-8965.
55. Stephen, M. J. (1957) Mol. Phys. 1, 223-232.
56. Taylor, H. C., Richardson, D. C., Richardson, J. S., Wlodawer, A., Komoriya, A., & Chaiken, I. M. (1981) J. Mol. Biol. 149, 313-317.
57. Warshel, A., & Creighton, S. (1989) Computer Simulation of Biomolecular Systems (van Gunsteren, W. F., & Weiner, P. K., Eds.) pp 120-138, ESCOM Science Publishers, Leiden.
58. Weiner, S. J., Kollman, P. A., Hguyen, D. T., & Case, D. A. (1986) J. Comput. Chem. 7, 230-252.