Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations

Biochemistry

Volumn 38, Issue 8, 1999, Pages 2340-2346

  Lee, Seok Yong ^a,c   Lee, Jung Hoon ^a   Chang, Ho Jin ^b   Cho, Joong Myung ^b   Jung, Jin Won ^a   Lee, Weontae ^a  

^a Yonsei University   (South Korea)

^b LG Chemical Ltd   (South Korea)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DIMER; ISOPROTEIN; MONELLIN; MONOMER;

AMINO ACID SEQUENCE; ANALYTIC METHOD; AQUEOUS SOLUTION; ARTICLE; HYDROGEN BOND; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; SWEETNESS;

ALGORITHMS; AMINO ACID SEQUENCE; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; MATHEMATICAL COMPUTING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; SWEETENING AGENTS; THERMODYNAMICS;

EID: 0033596696     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9822731     Document Type: Article

References (44)

1. van der Wel, H. (1976) Biochemistry of Sensory Functions 197, 235-242.
2. Morris, J. A., and Cagan, R. H. (1972) Biochim. Biophys. Acta 261, 114-122.
3. Cagan, R. H. (1984) Experientia 40, 843-844.
4. Kohmura, M., Nio, N., and Ariyoshi, Y. (1991) Agric. Biol. Chem. 55, 1831-1838.
5. Kohmura, M., Nio, N., and Ariyoshi, Y. (1992) Biosci. Biotechnol. Biochem. 561, 472-476.
6. Tancredi, T., Iijima, H., Saviano, G., Amodeo, P., and Temussi, P. A. (1992) FEBS Lett. 310, 27-30.
7. Kohmura, M., Nio, N., and Ariyoshi, Y. (1992) Biosci. Biotechnol. Biochem. 56, 1937-1942.
8. Somoza, J. R., Cho, J. M., and Kim, S. H. (1995) Chem. Senses 20, 61-68.
9. Tonosaki, K., Miwa, K., and Kanemura, F. (1997) Brain Res. 48, 234-236.
10. Hellekant, G., Glaser, D., Brouwer, J. N., and van der Wel, H. (1916) Acta Physiol. Scand. 97, 241-250.
11. Morris, J. A. (1976) Lloydia 39, 25-38.
12. Kurihara, K., and Beidler, L. M. (1968) Science 161, 1241-1243.
13. Liu, X., Maeda, S., Hu, Z., Aiuchi, T., Nakaya, K., and Kurihara, Y. (1993) Eur. J. Biochem. 211, 281-287.
14. van der Wel, H., and Loeve, K. (1972) Eur. J. Biochem. 31, 221-225.
15. Yamashita, H., Theerasilp, S., Aiuchi, T., Nakaya, K., Nakamura, Y., and Kurihara, Y. (1990) J. Biol. Chem. 265, 15770-15775.
16. Brouwer, J. N., Hellekant, G., Kasahara, Y., van der Wel, H., and Zotterman, Y. (1973) Acta Physiol. Scand. 89, 550-557.
17. Hough, C. A. M., and Edwardson, J. A. (1978) Nature 271, 381-383.
18. Ogata, C., Hatada, M., Tomlinson, G., Shin, W. C., and Kim, S. H. (1987) Nature 328, 739-742.
19. Fan, P., Bracken, C., and Baum, J. (1993) Biochemistry 32, 1573-1582.
20. Murzin, A. Z. (1993) J. Mol. Biol. 230, 689-694.
21. Kim, S. H., Kang, C. H., Kim, R., Cho, J. M., Lee, Y. B., and Lee, T. K. (1989) Protein Eng. 2, 571-575.
22. Somoza, J. R., Fan, J., Tong, L., Kang, C. H., Cho, J. M., and Kim, S. H. (1993) J. Mol. Biol. 234, 390-404.
23. Tomic, M. T., Somoza, J. R., Wemmer, D. E., Park, Y. W., Cho, J. M., and Kim, S. H. (1992) J. Biomol. NMR 2, 557-572.
24. Van Geet, A. L. (1970) Anal. Chem. 42, 679.
25. Piotto, M., Saudek, V., and Sklenar, V. (1992) J. Biomol. NMR 2, 661-665.
26. Lomize, A. L., Sobol', A. G., and Arsen'ev, A. S. (1990) Bioorg. Khim. 16, 179-201.
27. Suri, A. K., and Levy, R. M. (1995) J. Magn. Reson. 106, 24-31.
28. Bax, A., and Davis, D. G. (1985) J. Magn. Reson. 65, 355-360.
29. Rance, M., Soerensen, O. W., Bodehausen, G., Wagner, G., Ernest, R. R., and Wuthrich, K. (1983) Biochem. Biophys. Res. Commun. 117, 479-485.
30. Wuthrich, K., Billeter, M., and Braun, W. (1983) J. Mol. Biol. 169, 949-961.
31. Bodenhausen, G., and Ruben, D. J. (1980) Chem. Phys. Lett. 69, 185-189.
32. Kay, L. E., Keifer, P., and Saainen, T. (1992) J. Am. Chem. Soc. 114, 10663-10665.
33. Kay, L. E., and Bax, A. (1990) J. Magn. Reson. 86, 110-126.
34. Marion, D., Kay, L. E., Sparks, S. W., Torchia, D. A., and Bax, A. (1989) J. Am. Chem. Soc. 111, 1515-1517.
35. Marion, D., Driscoll, P. C., Kay, L. E., Wingfield, P. T., Bax, A., Gronenborn, A. M., and Clore, G. M. (1989) Biochemistry 28, 6150-6156.
36. Otting, G., Widmer, H., Wagner, G., and Wuthrich, K. (1988) J. Magn. Reson. 66, 187-193.
37. Nilges, M., Clore, G. M., and Gronenborn, A. M. (1988) FEBS Lett. 229, 317-324.
38. Nilges, M., Clore, G. M., and Gronenborn, A. M. (1988) FEBS Lett. 239, 129-136.
39. Lee, W., Moore, C. H., Watt, D. D., and Krishna, N. R. (1994) Eur. J. Biochem. 218, 89-95.
40. Wuthrich, K. (1986) NMR of Proteins and Nucleic Acids, John Wiley & Sons, New York.
41. Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., and Sykes, B. D. (1995) J. Biomol. NMR 5, 67-81.
42. Hyberts, S. G., Goldberg, M. S., Havel, T. F., and Wagner, G. (1992) Protein Sci. 1, 736-751.
43. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.
44. Mizukoshi, T., Kohmura, M., Suzuki, E., and Ariyoshi, Y. (1997) FEBS Lett. 413, 409-416.