Effects of Alanine and Glycine Substitution for Tryptophan on the Heterogeneity of Gramicidin a Analogs in Micelles

Journal of Magnetic Resonance

Volumn 124, Issue 1, 1997, Pages 132-139

  Hinton, J F ^a   Washburn McCain, A M ^a   Snow, A ^a   Douglas, J ^a  

^a UNIVERSITY OF ARKANSAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; DODECYL SULFATE SODIUM; GLYCINE; GRAMICIDIN; TRYPTOPHAN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; MICELLE; NUCLEAR MAGNETIC RESONANCE; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; GLYCINE; GRAMICIDIN; MICELLES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; SODIUM DODECYL SULFATE; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTOPHAN;

EID: 0030622211     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1996.7493     Document Type: Article

References (47)

1. D. W. Urry, Proc. Natl. Acad. Sci. USA 68, 672 (1971).
2. N. Jing, K. U. Prasad, and D. W. Urry, Biophys. J. 66, 353 (1994).
3. A. S. Arseniev, I. L. Barsukov, V. F. Bystrov, A. L. Lomize, and Y. A. Ovchinnikov, FEBS Lett. 186, 168 (1985).
4. V. F. Bystrov, A. S. Arseniev, I. L. Barsukov, and A. L. Lomize, Bull. Magn. Reson. 8, 84 (1986).
5. L. K. Nicholson, F. Moll, T. E. Mixon, P. V. LoGrosso, J. C. Lay, and T. A. Cross, Biochemistry 26, 6621 (1987).
6. B. A. Cornell, F. Separovic, A. J. Baldassi, and R. Smith, Biophys. J. 53, 67 (1988).
7. J. H. Davis, Biochemistry 27, 428 (1988).
8. L. K. Nicholson and T. A. Cross, Biochemistry 28, 9379 (1989).
9. R. Smith, D. E. Thomas, F. Separovic, A. R. Atkins, and B. A. Cornell, Biophys. J. 56, 307 (1989).
10. A. S. Arseniev, A. L. Lomize, I. L. Barsukov, and V. F. Bystrov, Biol. Membr. 3, 1077 (1986).
11. R. S. Prosser, J. H. Davis, F. W. Dahlquist, and M. A. Lindorfer, Biochemistry 30, 4687 (1991).
12. A. L. Lomize, V. Yu. Orekhov, and A. S. Arseniev, Bioorg. Khim. 18, 182 (1992).
13. W. Mai, W. Hu, C. Wang, and T. A. Cross, Protein Sci. 2, 532 (1993).
14. R. R. Ketchem, W. Hu, and T. A. Cross, Science 261, 1457 (1993).
15. O. S. Andersen, D. V. Greathouse, R. E. Koeppe, and L. L. Providence, Biophys. J. 61, A526 (1992).
16. D. B. Sawyer, R. E. Koeppe, and O. S. Andersen, Biophys. J. 57, 515 (1990).
17. E. K. Bamberg, K. Noda, E. Gross, and P. Lauger, Biochim. Biophys. Acta 419, 223 (1976).
18. F. Heitz, G. Spach, and Y. Trudelle, Biophys. J. 40, 87 (1982).
19. R. E. Koeppe, D. V. Greathouse, L. L. Providence, and O. S. Andersen, Biophys. J. 59, 319a (1991).
20. O. S. Andersen and R. E. Koeppe, Physiol. Rev. 72, S89 (1992).
21. H. Takeuchi, Y. Nemoto, and I. Harada, Biochemistry 29, 1572 (1990).
22. C. Etchebest and A. Pullman, J. Biomol. Struct. Dyn. 2, 859 (1985).
23. M. D. Becker, D. V. Greathouse, R. E. Koeppe, and O. S. Andersen, Biochemistry 30, 8830 (1991).
24. M. D. Becker, R. E. Koeppe, and O. S. Andersen, Biophys. J. 62, 25 (1992).
25. L. T. Boni, A. J. Connolly, and A. M. Kleinfeld, Biophys. J. 49, 122 (1986).
26. P. M. McDonald and J. Seelig, Biochemistry 27, 2357 (1988).
27. R. E. Koeppe, J. L. Mazet, and O. S. Andersen, Biochemistry 29, 512 (1990).
28. J. L. Mazet, O. S. Andersen, and R. E. Koeppe, Biophys. J. 45, 263 (1984).
29. J. T. Durkin, R. E. Koeppe, and O. S. Andersen, J. Mol. Biol. 211, 221 (1990).
30. R. E. Jacobs and S. H. White, Biochemistry 28, 3421 (1989).
31. P. Meers, Biochemistry 29, 3325 (1990).
32. A. Chattopadhyay and M. G. McNamee, Biochemistry 30, 7159 (1991).
33. M. Schiffer, C.-H. Chang, and F. J. Stevens, Protein Eng. 5, 213 (1992).
34. J. L. Fauchere, TIBS 10, 268 (1985).
35. R. Henderson, J. M. Baldwin, T. A. Cross, F. Zemlin, E. Beckmann, and K. H. Downing, J. Mol. Biol. 213, 899 (1990).
36. J. A. Ippolito, R. S. Alexander, and D. W. Christianson, J. Mol. Biol. 215, 457 (1990).
37. N. D. Lazo, W. Hu, and T. A. Cross, J. Chem. Soc. Chem. Commun. 1529 (1992).
38. S. F. Scarlata, Biochemistry 30, 9853 (1991).
39. A. M. O'Connell, R. E. Koeppe, and O. S. Andersen, Science 250, 1256 (1990).
40. G. H. W. M. Meulendijks, T. Sonderkamp, J. E. Dubois, R. J. Nielen, J. A. Kremers, and H. M. Buck, Biochem. Biophys. Acta 979, 321 (1989).
41. W. Hu, K.-C. Lee, and T. A. Cross, Biochemistry 32, 7035 (1993).
42. J. F. Hinton and A. M. Washburn, Biophys. J. 69, 435 (1995).
43. R. E. Koeppe and L. B. Weiss, J. Chromatogr. 208, 414 (1981).
44. R. E. Koeppe, J. A. Paczkowski, and W. L. Whaley, Biochemistry 24, 2822 (1985).
45. L. B. Weiss and R. E. Koeppe, Int. J. Peptide Protein Res. 26, 305 (1985).
46. P. A. McDonnell and S. J. Opella, J. Magn. Reson. B 102, 120 (1993).
47. M. L. Wilson and F. Dahlquist, Biochemistry 24, 1920 (1985).