Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin: Structural origin of sweetness

Journal of Biological Chemistry

Volumn 276, Issue 22, 2001, Pages 19624-19630

  Sung, Yoon Hui ^a   Shin, Joon ^a   Chang, Ho Jin ^b   Cho, Joong Myung ^b,c   Lee, Weontae ^a  

^a Yonsei University   (South Korea)

^b LG Chemical Ltd   (South Korea)

^c CrystalGenomics Inc   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; GENETIC ENGINEERING; LIQUID CHROMATOGRAPHY; MONOMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYPEPTIDES;

SINGLE-CHAIN MONELLIN (SCM);

PROTEINS;

ARGININE; ASPARAGINE; GLUTAMINE; MONELLIN; ASPARTIC ACID; GLUTAMIC ACID; MONELLIN PROTEIN, DIOSCOREOPHYLLUM CUMMINSII; SWEETENING AGENT; VEGETABLE PROTEIN;

ALPHA HELIX; AQUEOUS SOLUTION; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; GEL FILTRATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SPECTROFLUOROMETRY; SWEETNESS; CHEMICAL STRUCTURE; CHEMISTRY; GEL CHROMATOGRAPHY; GENETICS; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; TEMPERATURE;

ARGININE; ASPARTIC ACID; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; GLUTAMIC ACID; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; SWEETENING AGENTS; TEMPERATURE;

EID: 0035375110     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M100930200     Document Type: Article

References (39)

1. van der Wel, H. (1976) Biochem. Sensory Funct. 197, 235-242
2. Morris, J. A., and Cagan, R. H. (1972) Biochim. Biophys. Acta. 261, 114-122
3. Brouwer, J. N., Hellekant, G., Kasahara, Y., van der Wel, H., and Zotterman, Y. (1973) Acta Physiol. Scand. 89, 550-557
4. Hough, C. A. M., and Edwardson, J. A. (1978) Nature 271, 381-383
5. Hellekant, G., Glaser, D., Brouwer, J. N., and van der Wel, H. (1976) Acta Physiol. Scand. 97, 241-250
6. Morris, J. A. (1976) Lloydia 39, 25-38
7. Kurihara, K., and Beidler, L. M. (1968) Science 161, 1241-1243
8. Liu, X., Maeda, S., Hu, Z., Ajuchi, T., Nakaya, K., and Kurihara, Y. (1993) Eur. J. Biochem. 211, 281-287
9. van der Wel, H., and Loeve, K. (1972) Eur. J. Biochem. 12, 221-225
10. Yamadhita, H., Theerasilp, S., Ajuchi, T., Nakaya, K., Nakamura, Y., and Kurihara, Y. (1990) J. Biol. Chem. 265, 15770-15775
11. Ogata, C., Hatada, M., Tomlinson, G., Shin, W. C., and Kim, S. H. (1987) Nature 328, 739-742
12. Fan, P., Bracken, C., and Baum, J. (1993) Biochemistry 32, 1573-1582
13. Murzin, A. Z. (1993) J. Mol. Biol. 230, 689-694
14. Kim, S. H., Kang, C. H., Kim, R., Cho, J. M., Lee, Y. B., and Lee, T. K. (1989) Protein Eng. 2, 571-575
15. 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
16. Lee, S. Y., Lee, J. H., Chang, H. J., Cho, J. M., Jung, J. W., and Lee, W. (1999) Biochemistry 38, 2340-2346
17. Agashe, V. R., and Udgaonkar, J. B. (1995) Biochemistry 34, 3286-3299
18. Bodenhausen, G., and Ruben, D. J. (1980) Chem. Phys. Lett. 69, 185-189
19. Kay, L. E., Keifer, P., and Saainen, T. (1992) J. Am. Chem. Soc. 114, 10663-10665
20. Lomize, A. L., Sobol', A. G., and Arsen'ev, A. S. (1990) Bioorg. Khim. 16, 179-201
21. Suri, A. K., and Levy, R. M. (1995) J. Magn. Reson. 106, 24-31
22. Bax, A., and Davis, D. G. (1985) J. Magn. Reson. 65, 355-360
23. Marion, D., Kay, L. E., Sparks, S. W., Torchia, D. A., and Bax, A. (1989) J. Am. Chem. Soc. 111, 1515-1517
24. Krishnamurthy, V. V. (1995) J. Magn. Reson. 106, 170-177
25. Vuister, G. W., and Bax, A. (1993) J. Am. Chem. Soc. 115, 7772-7777
26. Rance, M., Soerensen, O. W., Bodehausen, G., Wagner, G., Ernst, R. R., and Wuthrich, K. (1983) Biochem. Biophys. Res. Commun. 117, 479-485
27. Kay, L. E., Torchia, D. A., and Bax, A. (1989) Biochemistry 28, 8972-8979
28. Skelton, N. J., Palmer, A. G., Akke, M., Kordel, J., Rance, M., and Chazin, W. J. (1993) J. Magn. Reson. 102, 253-264
29. Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., and Kay, L. E. (1994) Biachemistry 33, 5984-6003
30. Grzesiek, S., and Bax, A. (1993) J. Am. Chem. Soc. 115, 12593-12594
31. Nilges, M., Clore, G. M., and Gronenborn, A. M. (1988) FEBS Lett. 229, 317-324
32. Nilges, M., Clore, G. M., and Gronenborn, A. M. (1988) FEBS Lett. 239, 129-136
33. Lee, W., Moore, C. H., Watt, D. D., and Krishna, N. R. (1994) Eur. J. Biochem. 218, 89-95
34. Driscoll, P. C., Gronenborn, A. M., Beress, L., and Clore, G. M. (1989) Biochemistry 28, 2188-2198
35. Wuthrich, K., Billeter, M., and Braun, W. (1983) J. Mol. Biol. 169, 949-961
36. Clore, G. M., Gronenborn, A. M., Nilges, M., and Ryan, C. A. (1987) Biochemistry 26, 8012-8023
37. Wagner, G., Braun, W., Havel, T. F., Schaumann, T., Go, N., and Wuthrich, K. (1987) J. Mol. Biol. 196, 611-639
38. Krishnagopal, M., Swapan, K. B., Bireswar, C., and Roland, J. S. (1985) Biochim. Biophys. Acta 832, 156-164
39. Woody, R. W. (1978) Biopolymers 17, 1451-1467