In situ analysis of peptidyl DOPA in mussel byssus using rotational- echo double-resonance NMR

Archives of Biochemistry and Biophysics

Volumn 333, Issue 1, 1996, Pages 221-224

  Klug, Christopher A ^a,c   Burzio, Luis A ^b   Waite, J Herbert ^b   Schaefer, Jacob ^a  

^a WASHINGTON UNIVERSITY   (United States)

^b UNIVERSITY OF DELAWARE   (United States)

^c Stanford University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DOPA; TYROSINE;

ARTICLE; COVALENT BOND; CROSS LINKING; MUSSEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS;

EID: 0030249201     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1006/abbi.1996.0384     Document Type: Article

References (23)

1. 1. Waite, J. H. (1992) in Results and Problems in Cell Differentiation: 19 Biopolymers (Case, S. T., Ed.), PP. 27-54, Springer-Verlag, Berlin.
2. 2. Waite, J. H. (1990) Comp. Biochem. Physiol. 97B, 19-29.
3. 3. Holl, S. M., Hansen, D. C., Waite, J. H., and Schaefer, J. (1993) Arch. Biochem. Biophys. 302, 255-258.
4. 4. Gullion, T., and Schaefer, J. (1989a) J. Magn. Reson. 81, 196-200.
5. 5. Gullion, T., and Schaefer, J. (1989b) Adv. Mag. Reson. 13, 57-83.
6. 6. Gullion, T., Baker, D. B., and Conradi, M. S. (1990) J. Magn. Reson. 89, 479-484.
7. 7. Schmidt, A., McKay, R. A., and Schaefer, J. (1992) J. Magn. Reson. 96, 644-650.
8. 8. Schmidt, A., Kowalewski, T., and Schaefer, J. (1993) Macromolecules 26, 1729-1733.
9. 9. Schaefer, J., Kramer, K. J., Garbow, J. R., Jacob, G. S., Stejskal, E. O., Hopkins, T. L., and Speirs, R. D. (1987) Science 235, 1200-1204.
10. 10. Waite, J. H., and Tanzer, M. L. (1980) Biochem. Biophys. Res. Commun. 96, 1554-1561.
11. 11. Taylor, S. W., Luther, G., and Waite, J. H. (1994) Inorg. Chem. 33, 5819-5824.
12. 12. Andersen, S. O. (1966) Acta Physiol. Scand. Suppl. 263 66, 1-81.
13. 13. Foerder, C. S., and Shapiro, B. M. (1977) Proc. Natl. Acad. Sci. USA 74, 4214-4218.
14. 14. Fujimoto, D., Horiuchi, K., and Hirama, M. (1981) Biochem. Biophys. Res. Commun. 99, 637-643.
15. 15. Fry, S. C. (1982) Biochem. J. 204, 449-455.
16. 16. Epstein, L., and Lamport, D. T. A. (1984) Phytochemistry 23, 1241-1246.
17. 17. Nomura, K., Suzuki, N., and Matsumoto, S. (1990) Biochemistry 29, 4525-4534.
18. 18. Everdeen, D. S., Kiefer, S., Willard, J. J., Muldoon, E. P., Dey, P. M., Li, S. B., and Lamport, D. T. A. (1988) Plant Physiol. 87, 616-621.
19. 19. Rzepecki, L. M., Qin, X. X., Waite, J. H., and Lavin, M. F. (1990) Mol. Mar. Biol. Biotechnol. 1, 78-88.
20. 20. Papov, V. V., Diamond, T. V., Biemann, K., and Waite, J. H. (1995) J. Biol. Chem. 270, 20183-20192.
21. 21. Andersen, S. O., Jacobsen, J. P., Bojesen, G., and Roepstorff, P. (1992) Biochim. Biophys. Acta 1118, 134-138.
22. 22. Dougherty, D. A. (1996) Science 271, 163-168.
23. 23. Dolmer, P., and Svane, I. (1994) Ophelia 40, 63-74.