Structure and function of an aromatic ensemble that restricts the dynamics of the hydrophobic cork of a designed helix-loop-helix dimer

Journal of the American Chemical Society

Volumn 119, Issue 37, 1997, Pages 8598-8607

  Brive, Lars ^a   Dolphin, Gunnar T ^a   Baltzer, Lars ^a  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

HELIX LOOP HELIX PROTEIN; POLYPEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; DISSOCIATION CONSTANT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

EID: 0030885116     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja970477j     Document Type: Article

References (57)

1. Ho, S.; DeGrado, W. J. Am. Chem. Soc. 1987, 109, 6751-6758.
2. Olofsoon, S.; Johansson, G.; Baltzer, L. J. Chem. Soc., Perkin Trans. 2 1995, 2047-2056.
3. Kaumaya, P. T. P.; Berndt, K. D.; Heidorn, D. B.; Trewhella, J.; Kezdy, F. J.; Goldberg, E. Biochemistry 1990, 29, 13-23.
4. Raleigh, D. P.; Betz, S.; DeGrado, W. F. J. Am. Chem. Soc. 1995, 117, 7558-7559.
5. Dolphin, G. T.; Brive, L.; Johansson, G.; Baltzer, L. J. Am. Chem. Soc. 1996, 118, 11297-11298.
6. Betz, S. F.; DeGrado, W. F. Biochemistry 1996, 35, 6955-6962.
7. Quinn, T. P.; Tweedy, N. B.; Williams, R. W.; Richardson, J. S.; Richardson, D. C. Proc. Nat. Acad. Sci. 1994, 91, 8747-8751.
8. Struthers, M. D.; Cheng, R. P.; Imperiali, B. Science 1996, 271, 342-345.
9. Struthers, M. D.; Cheng, R. P.; Imperiali, B. J. Am. Chem. Soc. 1996, 118, 3073-3081.
10. Mutter, M.; Vuilleumier, S. Angew. Chem., Int. Ed. Engl. 1989, 28, 535-676.
11. Bryson, J. W.; Betz, S. F.; Lu, H. S.; Suich, D. J.; Zhou, H. X.; O'Neil, K. T.; DeGrado, W. F. Science 1995, 270, 935-941.
12. Handel, T. M.; Williams, S. A.; DeGrado, W. F. Science 1993, 261, 879-885.
13. Levitt, M. Biochemistry 1978, 17, 4277-4284.
14. Richardson, J.; Richardson, D. In Prediction of protein structure and the principles of protein conformation; Fasman, G., Ed.; Plenum Press: New York, 1989; pp 1-98.
15. Abbreviations: Nva, L-norvaline; Aad, L-α-aminoadipic acid; ANS, 8-anilino-l-naphthalenesulfonic acid; CD, circular dichroism; NMR, nuclear magnetic resonance; TOCSY, totally correlated spectroscopy; NOESY, nuclear Overhauser enhancement spectroscopy; DQF-COSY, double quantum filtered correlated spectroscopy; TFA, trifluoroacetic acid; DCM, dichloromethane; TFE, 2,2,2-trifluoroethanol.
16. Presta, L. G.; Rose, G. D. Science 1988, 240, 1632-1641.
17. Serrano, L.; Fersht, A. Nature 1989, 542, 296-299.
18. Shoemaker, K.; Kim, P.; York, E.; Stewart, J.; Baldwin, R. Nature 1987, 326, 563-567.
19. Merutka, G.; Stellwagen, E. Biochemistry 1991, 30, 1591-1594.
20. Hodges, R. S. Biochem. Cell Biol. 1996, 74, 133-154.
21. Chothia, C.; Levitt, M.; Richardson, D. J. Mol. Biol. 1981, 145, 215-250.
22. Lyu, P.; Sherman, J.; Chen, A.; Kallenbach, N. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 5317-5320.
23. Padmanabhan, S.; Baldwin, R. J. Mol. Biol. 1991, 219, 135-137.
24. Sheridan, R. P. Proc. Nat. Acad. Sci. 1982, 79, 4545-4549.
25. Stewart, J. M.; Young, J. D. Solid Phase Peptide Synthesis; Pierce Chemical Co.: Ruckford, IL, 1984.
26. Johnson, W. C. J. Ann. Rev. Biophys. Biophys. Chem. 1988, 17, 145-166.
27. Nelson, J.; Kallenbach, N. Proteins 1986, 1, 211-217.
28. Hyberts, S. G.; Märki, W.; Wagner, G. Eur. J. Biochem 1987, 164, 625-635.
29. Constantine, K. L.; Friedrichs, M. S.; Mueller, L. J. Magn. Reson. 1994, 104, 62-68.
30. Cai, M.; Liu, J.; Gong, Y.; Krishnamoorthi, R. J. Magn. Reson. 1995, 107, 172-178.
31. Wishart, D. S.; Sykes, B. D. Methods in Enzymology 239; Academic Press: San Diego, CA, 1993; pp 363-392.
32. Wüthrich, K. Science 1989, 243, 45-50.
33. Zhou, N. E.; Zhu, B.; Sykes, B. D.; Hodges, R. S. J. Am. Chem. Soc. 1992, 114, 4320-4326.
34. Brünger, A. T. X-PLOR Version 3.1. A System for X-ray Crystallography and NMR; Yale University Press: New Haven, CT, 1992.
35. Lakowicz, Y. Principles of Fluorecence Spectroscopy; Plenum Press: New York, 1983.
36. Shinitzky, M.; Goldman, R. J. Biochem. 1967, 3, 139-144.
37. Steiner, R. F.; Kirby, E. P. J. Phys. Chem. 1969, 73, 4130-4135.
38. Bushueva, T. L.; Basel, E. P.; Bushueva, V. N.; Burstein, E. A. Stud. Biophys. 1974, 44, 129-139.
39. Dolphin, G. T.; Baltzer, L. Unpublished results.
40. Pace, C. N. Methods Enzymol. 1986, 131, 266-280.
41. DeFrancesco, R.; Pastore, A.; Vecchio, G.; Cortese, R. Biochemistry 1991, 30, 143-147.
42. Bai, Y.; Milne, J. S.; Mayne, L.; Englander, S. W. Proteins 1993, 17, 75-86.
43. Olofsson, S.; Baltzer, L. Folding Des. 1996, 1, 347.
44. Semisotnov, G.; Rodionova, N.; Razgulyaev, O.; Uversky, V.; Gripas, A.; Gilmanshin, R. Biopolymers 1991, 31, 119-128.
45. Cooper, T.; Woody, R. Biopolymers 1990, 30, 657-676.
46. Zhou, N.; Zhu, B.; Kay, C.; Hodges, R. Biopolymers 1992, 32, 419-426.
47. Lundh, A.-C.; Broo, K.; Baltzer, L. J. Chem. Soc., Perkin Trans. 2 In press.
48. Powers, R.; Garret, D. S.; March, C. J.; Frieden, E. A.; Gronenborn, A. M.; Clore G. M. Biochemistry 1992, 31, 4334-4346.
49. Kuroda, Y.; Nakai, T.; Ohkubo, T. J. Mol. Biol. 1994, 236, 862-868.
50. Sancho, J.; Neira, J. L.; Fersht, A. R. J. Mol. Biol. 1992, 224, 749-758.
51. Buck, M.; Radford, R. S.; Dobson, C. M. Biochemistry 1993, 32, 669-678.
52. Desjarlais, J. R.; Handel, T. M. Protein Sci. 1995, 4, 2006-2018.
53. Zhou, N.; Kay, C.; Hodges, R. J. Biol. Chem. 1992, 267, 2664-2670.
54. Tam, J. P.; Heath, W. F.; Merrifield, R. B. J. Am. Chem. Soc. 1983, 105, 6442-6455.
55. Shields, J.; McGregor, W.; Carpenter, F. J. Am. Chem. Soc. 1961, 26, 1491-1494.
56. Prestidge, R., Harding, D.; Battersby, J.; Hancock, W. J. Org. Chem. 1975, 40, 3287-3288.
57. Ledger, R.; Stewart, F. Aust. J. Chem. 1965, 18, 1477-1484.