Interactions involved in the realignment of membrane-associated helices: An investigation using oriented solid-state NMR and attenuated total reflection Fourier transform infrared spectroscopies

Journal of Biological Chemistry

Volumn 281, Issue 12, 2006, Pages 7708-7716

  Aisenbrey, Christopher ^a,b   Kinder, Rudolf ^b   Goormaghtigh, Erik ^c   Ruysschaert, Jean Marie ^c   Bechinger, Burkhard ^a,b  

^a UNIVERSITÉ DE STRASBOURG   (France)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DNA; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MICELLES; NITROGEN COMPOUNDS; NUCLEAR MAGNETIC RESONANCE; PH EFFECTS;

HELICAL SEQUENCES; MEMBRANE INTERACTIONS; MEMBRANE-ASSOCIATED HELICES; RESIDUE TRANSITIONS;

BIOLOGICAL MEMBRANES;

ALANINE; AMINO ACID; GLYCINE; HISTIDINE; LEUCINE; POLYPEPTIDE; TRYPTOPHAN; TYROSINE; DETERGENT; DNA; PEPTIDE; PROTON;

ARTICLE; DNA TRANSFECTION; HYDROPHOBICITY; INFRARED SPECTROSCOPY; MEMBRANE POTENTIAL; MICELLE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMICAL MODEL; CHEMISTRY; GENETIC TRANSFECTION; LIPID BILAYER; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SPECTROPHOTOMETRY; STATISTICAL MODEL; THERMODYNAMICS;

ALANINE; AMINO ACID SEQUENCE; CELL MEMBRANE; DETERGENTS; DNA; GLYCINE; HISTIDINE; HYDROGEN-ION CONCENTRATION; LEUCINE; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MICELLES; MODELS, CHEMICAL; MODELS, STATISTICAL; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; PROTONS; SPECTROPHOTOMETRY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS; TRANSFECTION; TRYPTOPHAN; TYROSINE;

EID: 33646378678     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M513151200     Document Type: Article

References (65)

1. Chen, C. P., and Rost, B. (2002) Appl. Bioinform. 1, 1-15
2. Wimley, W. C., and White, S. H. (1996) Nat. Struct. Biol. 3, 842-848
3. Hessa, T., Kim, H., Bihlmaier, K., Lundin, C., Boekel, J., Andersson, H., Nilsson, I., White, S. H., and von Heijne, G. (2005) Nature 433, 377-381
4. von Heijne, G. (1981) Eur. J. Biochem. 120, 275-278
5. Kyte, J., and Doolittle, R. F. (1982) J. Mol. Biol. 157, 105-132
6. Rees, D. C., DeAntonio, L., and Eisenberg, D. (1989) Science 245, 510-513
7. Engelman, D. M., Steitz, T. A., and Goldman, A. (1986) Annu. Rev. Biophys. Biophys. Chem. 15, 321-353
8. Moller, S., Kriventseva, E. V., and Apweiler, R. (2000) Bioinformatics 16, 1159-1160
9. Degli, E. M., Crimi, M., and Venturoli, G. (1990) Eur. J. Biochem. 190, 207-219
10. Gromiha, M. M., and Ponnuswamy, P. K. (1996) Int. J. Pept. Protein Res. 48, 452-460
11. Jones, D. T., Taylor, W. R., and Thornton, J. M. (1994) Biochemistry 33, 3038-3049
12. Punta, M., and Maritan, A. (2003) Proteins 50, 114-121
13. Promponas, V. J., Palaios, G. A., Pasquier, C. M., Hamodrakas, J. S., and Hamodrakas, S. J. (1999) In Silico Biol. 1, 159-162
14. Ikeda, M., Arai, M., Lao, D. M., and Shimizu, T. (2002) In Silico Biol. 2, 19-33
15. Jayasinghe, S., Hristova, K., and White, S. H. (2001) J. Mol. Biol. 312, 927-934
16. Chen, C. P., Kernytsky, A., and Rost, B. (2002) Protein Sci. 11, 2774-2791
17. Kall, L., and Sonnhammer, E. L. (2002) FEBS Lett. 532, 415-418
18. von Heijne, G. (1992) J. Mol. Biol. 225, 487-494
19. Sonnhammer, E. L., von Heijne, G., and Krogh, A. (1998) Proc. Int. Conf. Intell. Syst. Mol. Biol. 6, 175-182
20. Tusnady, G. E., and Simon, I. (1998) J. Mol. Biol. 283, 489-506
21. Hessa, T., White, S. H., and von Heijne, G. (2005) Science 307, 1427
22. Bechinger, B. (2001) FEBS Lett. 504, 161-165
23. Vogt, T. C. B., and Bechinger, B. (1999) J. Biol. Chem. 274, 29115-29121
24. Kichler, A., Leborgne, C., März, J., Danos, O., and Bechinger, B. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 1564-1568
25. Zakharov, S. D., Lindeberg, M., Griko, Y., Salamon, Z., Tollin, G., Prendergast, F. G., and Cramer, W. A. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 4282-4287
26. Losonczi, J. A., Olejniczak, E. T., Betz, S. F., Harlan, J. E., Mack, J., and Fesik, S. W. (2000) Biochemistry 39, 11024-11033
27. Bechinger, B. (1996) J. Mol. Biol. 263, 768-775
28. Kichler, A., Bechinger, B., and Danos, O. (2003) Med. Sci. 19, 1046-1047
29. Ladokhin, A. S., and White, S. H. (2004) Biochemistry 43, 5782-5791
30. Bechinger, B., and Sizun, C. (2003) Concepts Magn. Reson. 18A, 130-145
31. Bechinger, B., Ruysschaert, J. M., and Goormaghtigh, E. (1999) Biophys. J. 76, 552-563
32. Bechinger, B., Aisenbrey, C., and Bertani, P. (2004) Biochim. Biophys. Acta 1666, 190-204
33. Ivanov, D., Dubreuil, N., Raussens, V., Ruysschaert, J. M., and Goormaghtigh, E. (2004) Biophys. J. 87, 1307-1315
34. Goormaghtigh, E., Raussens, V., and Ruysschaert, J. M. (1999) Biochim. Biophys. Acta 1422, 105-185
35. Lopes, S. C., Goormaghtigh, E., Cabral, B. J., and Castanho, M. A. (2004) J. Am. Chem. Soc. 126, 5396-5402
36. Goormaghtigh, E., Cabiaux, V., and Ruysschaert, J. M. (1994) Subcell. Biochem. 23, 405-450
37. Goormaghtigh, E., Cabiaux, V., and Ruysschaert, J. M. (1990) Eur. J. Biochem. 193, 409-420
38. Aisenbrey, C. (2003) Étude Topologique de Polypeptides Membranaires par RMN du Solide et Spectroscopie Infrarouge par Réflexion Totale Attenuée. Ph.D. thesis, University Louis Pasteur, Strasbourg, France
39. Israelachvilli, J. N., Marcelja, S., and Horn, R. G. (1980) Q. Rev. Biophys. 13, 121-200
40. Atherton, E., Logan, C. J., and Sheppart, R. C. (1981) J. Chem. Soc. Perkin Trans. I 538-546
41. Carpino, L. A., and Han, G. Y. (1972) J. Org. Chem. 37, 3404
42. Griesinger, C., Otting, G., Wüthrich, K., and Ernst, R. R. (1988) J. Am. Chem. Soc. 110, 7870-7872
43. Macura, S., and Ernst, R. R. (1980) Mol. Phys. 41, 95-117
44. Piotto, M., Saudek, V., and Sklenar, V. (1992) J. Biomol. NMR 2, 661-665
45. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, John Wiley & Sons, Inc., New York
46. Bechinger, B., and Opella, S. J. (1991) J. Magn. Reson. 95, 585-588
47. Pines, A., Gibby, M. G., and Waugh, J. S. (1973) J. Chem. Phys. 59, 569-590
48. Zhang, Y. P., Ruthven, N. A. H. L., Hodges, R., and McElhaney, R. N. (1995) Biochemistry 34, 2362-2371
49. Zhang, Y. P., Lewis, R. N., Henry, G. D., Sykes, B. D., Hodges, R. S., and McElhaney, R. N. (1995) Biochemistry 34, 2348-2361
50. Vogt, T. C. B., Ducarme, P., Schinzel, S., Brasseur, R., and Bechinger, B. (2000) Biophys. J. 79, 2644-2656
51. Harzer, U., and Bechinger, B. (2000) Biochemistry 39, 13106-13114
52. Goormaghtigh, E., and Ruysschaert, J. M. (1990) in Molecular Description of Biological Membranes by Computer Aided Conformational Analysis (Brasseur, R., ed) pp. 285-332, CRC Press, Inc., Boca Raton, FL
53. Bechinger, B. (2001) Biophys. J. 82, 2251-2256
54. Mouritsen, O. G., and Bloom, M. (1984) Biophys. J. 46, 141-153
55. Killian, J. A. (1998) Biochim. Biophys. Acta 1376, 401-416
56. Chatelier, R. C., and Minton, A. P. (1996) Biophys. J. 71, 2367-2374
57. Zuckermann, M. J., and Heimburg, T. (2001) Biophys. J. 81, 2458-2472
58. White, S. H., and Wimley, W. C. (1999) Annu. Rev. Biophys. Biomol. Struct. 28, 319-365
59. Yau, W. M., Wimley, W. C., Gawrisch, K., and White, S. H. (1998) Biochemistry 37, 14713-14718
60. Killian, J. A., and von Heijne, G. (2000) Trends Biochem. Sci. 25, 429-434
61. White, S. H. (1994) in Membrane Protein Structure: Experimental Approaches (White, S. H., ed) pp. 3-26, Oxford University Press, New York
62. Deber, C. M., Wang, C., Liu, L. P., Prior, A. S., Agrawal, S., Muskat, B. L., and Cuticchia, A. J. (2001) Protein Sci. 10, 212-219
63. Pilpel, Y., Ben-Tal, N., and Lancet, D. (1999) J. Mol. Biol. 294, 921-935
64. Henry, B., Tekely, P., and Delpuech, J. J. (2002) J. Am. Chem. Soc. 124, 2025-2034
65. Gardiennet, C., Henry, B., Kuad, P., Spiess, B., and Tekely, P. (2005) Chem. Commun. (Camb.) 2, 180-182