NMR analysis of synthetic human serum albumin α-helix 28 identifies structural distortion upon amadori modification

Journal of Biological Chemistry

Volumn 280, Issue 24, 2005, Pages 22582-22589

  Howard, Mark J ^a   Mark Smales, C ^a  

^a UNIVERSITY OF KENT   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DISEASE CONTROL; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE; POLYPEPTIDES; SUGARS;

GLYCATION; HUMAN SERUM; NON-ENZYMATIC; PEPTIDES;

PROTEINS;

ADVANCED GLYCATION END PRODUCT; LYSINE; SERUM ALBUMIN; TRIFLUOROETHANOL;

AGING; ALPHA HELIX; ALZHEIMER DISEASE; AMADORI REARRANGEMENT; ARTICLE; DIABETES MELLITUS; GLYCATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; GLUCOSE; GLYCOSYLATION; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMANS; HYDROGEN BONDING; LYSINE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MODELS, MOLECULAR; PEPTIDES; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SERUM ALBUMIN; TEMPERATURE; TRIFLUOROETHANOL;

EID: 20744453679     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M501480200     Document Type: Article

References (37)

1. Lapolla, A., Fedele, D., Plebani, M., Aronica, R., Garbeglio, M., Seraglia, R., Dalpaos, M., and Traldi, P. (1999) Clin. Chem. 45, 288-290
2. Smales, C. M., Pepper, D. S., and James, D. C. (2002) Biotechnol. Bioeng. 77, 37-48
3. Smales, C. M., Pepper, D. S., and James, D. C. (2000) Biotechnol. Appl. Biochem. 32, 109-119
4. Alikhani, Z., Alikhani, M., Boyd, C., Nagao, K., Trackman, P. C., and Graves, D. T. (2005) J. Biol. Chem. 280, 12087-12095
5. Bucala, R. (1996) Diagn. Endocrin. Metab. 14, 99-106
6. Suarez, G., Rajaram, R., Oronsky, A. L., and Gawinowicz, M. A. (1989) J. Biol. Chem. 264, 3674-3679
7. Biemel, K. M., Friedl, D. A., and Lederer, M. O. (2002) J. Biol. Chem. 277, 24907-24915
8. Choi, Y.-G., Kim, J.-I., Jeon, Y.-C., Park, S.-J., Choi, E.-K., Rubenstein, R., Kascsak, R. J., Carp, R. I., and Kim, Y.-S. (2004) J. Biol. Chem. 279, 30402-30409
9. Davis, P. J., Smales, C. M., and James, D. C. (2001) Allergy 56, 56-60
10. Hanford, L. E., Enghild, J. J., Valnickova, Z., Petersen, S. V., Schaefer, L. M., Schaefer, T. M., Reinhart, T. A., and Oury, T. D. (2004) J. Biol. Chem. 279, 50019-50024
11. Sell, D. R., and Monnier, V. M. (2004) J. Biol. Chem. 279, 54173-54184
12. Blakytny, R., Carver, J. A., Harding, J. J., Kilby, G. W., and Sheil, M. M. (1997) Biochim. Biophys. Acta 1343, 299-315
13. Neglia, C., Cohen, H., Garber, A., Thorpe, S., and Baynes, J. (1985) J. Biol. Chem. 260, 5406-5410
14. Yoon, M. S., Jankowski, V., Montag, S., Zidek, W., Henning, L., Schluter, H., Tepel, M., and Jankowski, J. (2004) Biochem. Biophys. Res. Commun. 323, 377-381
15. Zigrovic, I., Kidric, J., and Horvat, S. (1998) Glycoconj. J. 15, 563-570
16. Shaklai, N., Garlick, R., and Bunn, H. (1984) J. Biol. Chem. 259, 3812-3817
17. Bunk, D. M. (1997) Anal. Chem. 69, 2457-2463
18. Wada, Y. (1996) J. Mass Spectrom. 31, 263-266
19. Zhao, H. R., Smith, J. B., Jiang, X. Y., and Abraham, E. C. (1996) Biochem. Biophys. Res. Commun. 229, 128-133
20. Munoz, V., and Serrano, L. (1995) J. Mol. Biol. 245, 275-296
21. Munoz, V., and Serrano, L. (1994) Nat. Struct. Biol. 1, 399-409
22. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293
23. Johnson, B. A., and Blevins, R. A. (1994) J. Biomol. NMR 4, 603-614
24. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905-921
25. Koradi, R., Billeter, M., and Wuthrich, K. (1996) J. Mol. Graph. 14, 51-55
26. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) J. Biomol. NMR 8, 477-486
27. van Gunsteren, W. F., Brunne, R. M., Gros, P., van Schaik, R. C., Schiffer, C. A., and Torda, A. E. (1994) Methods Enzymol. 239, 619-654
28. Guex, N., and Peitsch, M. C. (1997) Electrophoresis 18, 2714-2723
29. Rohovec, J., Maschmeyer, T., Aime, S., and Peters, J. A. (2003) Chemistry 9, 2193-2199
30. Cavanagh, J., Fairbrother, W. J., Palmer, A. G., and Skelton, N. J. (1996) Protein NMR Spectroscopy: Principles and Practice, Academic Press, Orlando, FL
31. Smales, C. M., Pepper, D. S., and James, D. C. (2000) Biotechnol. Bioeng. 67, 177-188
32. Wishart, D. S., and Sykes, B. D. (1994) Methods Enzymol. 239, 363-392
33. Wuthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley Interscience, New York
34. Williamson, R. A., Muskett, F. W., Howard, M. J., Freedman, R. B., and Carr, M. D. (1999) J. Biol. Chem. 274, 37226-37232
35. Arumugam, S., Gao, G., Patton, B. L., Semenchenko, V., Brew, K., and Van Doren, S. R. (2003) J. Mol. Biol. 327, 719-734
36. Coussons, P. J., Jacoby, J., McKay, A., Kelly, S. M., Price, N. C., and Hunt, J. V. (1997) Free Radic. Biol. Med. 22, 1217-1227
37. Ahmed, N., Dobler, D., Dean, M., and Thornalley, P. J. (2005) J. Biol. Chem. 280, 5724-5732