Application of the disulfide trapping approach to explain the antiparallel assembly of dimeric rabbit uteroglobin: A preliminary study using short peptide models

Letters in Peptide Science

Volumn 6, Issue 2-3, 1999, Pages 165-172

  Ferrer, Tina ^a   Nicolás, Ernesto ^a   Giralt, Ernest ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

Author keywords

Circular dichroism; Disulfide; Molecular recognition; Uteroglobin; helix

Indexed keywords

UTEROGLOBIN;

ARTICLE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; DISULFIDE BOND; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NONHUMAN; PEPTIDE ANALYSIS; PROTEIN STRUCTURE; RABBIT;

EID: 0032965852     PISSN: 09295666     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02443632     Document Type: Article

References (22)

1. a. Kazmierski, W.M. and McDermed, J., In Maia, H.L.S. (Ed.) Peptides: Chemistry, Structure and Biology (Proceedings of the 23th European Peptide Symposium), ESCOM, Leiden, 1995, pp. 52-53.
2. b. Royo, M., Albericio, F., Giralt, E. and Pons, M., In Maia, H.L.S. (Ed.) Peptides: Chemistry, Structure and Biology (Proceedings of the 23th European Peptide Symposium), ESCOM, Leiden, 1995, pp. 83-84.
3. Miele, L., Cordella-Miele, E., Mantile, G., Peri, A. and Mukherjee, A.B., J. Endocrinol. Invest., 17 (1994) 679.
4. a. Morize, I., Surcouf, E., Vaney, M.C., Epelboin, Y., Buehner, M., Fridlansky, F., Milgrom, E. and Morton, J.P., J. Mol. Biol., 194 (1987) 725.
5. b. Bally, R. and Delettré J., J. Mol. Biol., 206 (1989) 153.
6. Umland, T.C., Swaminathan, S., Furrey, W., Singh, G., Pletcher, J. and Sax, M., J. Mol. Biol., 224 (1992) 441.
7. Umland, T.C., Swaminathan, S., Singh, G., Warty, V., Furey, W., Pletcher, J. and Sax, M., Struct. Biol., 1 (1994) 538.
8. e. Hard, T., Barnes, H.J., Larsson, C., Gustafsson, J. and Lund, A.J., Nat. Struct. Biol., 2 (1995) 983.
9. a. Westphal, U., Monogr. Endocrinol., 27 (1986) 357.
10. b. López de Haro, M. S., Pérez Martínez, M., García, C. and Nieto, A., FEBS Lett., 349 (1994) 249.
11. Díaz González, K., Nieto, A., FEBS Lett., 361 (1995) 255.
12. Zhang, Z., Kundu, G. C., Yuan, C. J., Ward, J. M., Lee, E. J., DeMayo, F., Westphal, H. and Mukherjee, A. B., Science, 276 (1997) 1408.
13. Lin, S.L., Tsai, C. J. and Nussinov, R., J. Mol. Biol., 248 (1995) 151.
14. Miele, L., Cordella-Miele, E. and Mukherjee, A.B., Endocr. Rev., 8 (1987) 474.
15. Nicolas, E., Bacardit, J., Ferrer, T. and Giralt, E., Lett. Pept. Sci., 2 (1995) 353.
16. Lloyd-Williams, P., Albericio, F. and Giralt, E., Chemical Approaches to the Synthesis Of Peptides and Proteins, CRC Press, Boca Raton, FL, 1997, pp. 19-94.
17. Tam, J.P., Heath, W.F. and Merrifield, R.B., J. Am. Chem. Soc., 105 (1985) 6442.
18. Nicolas, E., Vilaseca, M. and Giralt, E., Tetrahedron, 51 (1995) 5701.
19. Chen, Y.H., Yang, J.T. and Chau, H., Biochemistry, 13 (1974) 3350.
20. Andreu, D., Albericio, F., Solé, N. A., Munson, M. C., Ferrer, M. and Barany G., In Pennington, M.W and Dunn, B.M. (Eds.) Methods in Molecular Biology, Vol. 35, Humana Press, Totowa, N.J., 1994, pp. 91-169.
21. Freinberg, J., Heitz, F., Benyamin, Y and Roustan, C., Biochem. Biophys. Res. Commun., 222 (1996) 127.
22. Fragments 4-14 and 49-65 of the monomer of uteroglobin had the same helical behaviour under micellar conditions: Tessari, M., Foffani, M.T., Mammi, S. and Peggion, E., Biopolymers, 33 (1993) 1877.