SDS-induced conformational transitions of ervatamin B: Evidence of greater stability of α-rich domain compared to β-rich domain of the SDS derived state

Colloids and Surfaces B: Biointerfaces

Volumn 32, Issue 3, 2003, Pages 223-234

  Bhowmick, Reshma ^a,b   Jagannadham, Medicherla V ^a  

^a BANARAS HINDU UNIVERSITY   (India)

^b MEDICAL COLLEGE OF WISCONSIN   (United States)

Author keywords

Cooperative transitions; Ervatamin B; Intermediate; SDS induced state

Indexed keywords

CONCENTRATION (PROCESS); FLUORESCENCE; PROTEINS; STRUCTURE (COMPOSITION);

FUNCTIONAL CHANGES;

SODIUM COMPOUNDS;

8 ANILINO 1 NAPHTHALENESULFONIC ACID; CYSTEINE PROTEINASE; DODECYL SULFATE SODIUM; ERVATIMIN B; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

ALPHA CHAIN; ALPHA HELIX; ARTICLE; BETA CHAIN; BINDING ASSAY; BIOLOGICAL MONITORING; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; FLUORESCENCE; MOLECULE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; TEMPERATURE DEPENDENCE;

EID: 0142200382     PISSN: 09277765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0927-7765(03)00160-7     Document Type: Article

References (55)

1. Reynolds J.A., Tanford C. Proc. Natl. Acad. Sci. USA. 66:1970;1002.
2. Ibel K., May R.P., Kirschner K., Szadkowski H., Mascher E., Lundahl P. Eur. J. Biochem. 190:1990;311.
3. Nelson C.A. J. Biol. Chem. 264:1971;3895.
4. Mikulska J., Boratynski J., Neizgodka M., Lisowski J. Immunol. Lett. 5:1982;137.
5. Hirai M., Kawai-Hirai R., Hirai T., Ukei T. Eur. J. Biochem. 215:1993;55.
6. Halfman C.J., Dowe R., Jay D.W., Scheneider A.S. Mol. Immunol. 23:1986;943.
7. Rao K.S., Prakash V. J. Biol. Chem. 268:1993;14769.
8. Yamasaki M., Yano H., Akoi K. Int. J. Biol. Macromol. 14:1992;305.
9. Lapenje S. Physicochemical Aspects of Protein Denaturation. 1978;10 Wily-Interscience Publication, New York.
10. Creighton T.E. Curr. Opin. Struct. Biol. 1:1991;5.
11. Ptitsyn O.B. Creighton T.E. Protein Folding. 1992;243 Freeman and Co, New York.
12. Dobson C.M., Fresht A.R. Protein Folding, Royal Society Meeting. 1995;Cambridge University Press, London.
13. Garel J.R. Creighton T.E. Protein Folding. 1992;405 Freeman Co, New York.
14. Price N.C. Pain R.H. Mechanisms of Protein Folding. 1993;16 IRL Press, New York.
15. Baldwin R.L. Chemtracts-Biochem. Mol. Biol. 2:1991;379.
16. Dobson C.M. Curr. Opin. Struct. Biol. 2:1992;6.
17. Sundd M., Kundu S., Jagannadham M.V. J. Biochem. Mol. Biol. 35:(2):2002;143.
18. Sundd M., Kundu S., Jagannadham M.V. J. Biochem. Mol. Biol. 35:(2):2002;155.
19. Kundu S., Sundd M., Jagannadham M.V. J. Agric. Food Chem. 48:2000;171.
20. Balasubramaniam D., Kumar C. Appl. Spectrosc. Rev. 11:1976;223.
21. Pace C.N., Shirley B.A., Thomson J.A. Creighton T.E. Protein Structure: A Practical Approach. 1989;311 IRL Press, Oxford, UK.
22. Stryer L. J. Mol. Biol. 13:1965;482.
23. Van der Goot F.G., Ausio J., Wong K.R., Pattus F., Buckley J.T. J. Biol. Chem. 268:1993;18272.
24. Jones M.N., Brass A. Dickson E. Food Polymers, Gels and Colloides. 1991;65 Royal Society of Chemistry, Cambridge.
25. Ananthapadmanabhan K.P. Ananthapadmanabhan K.P., Goddard E.D. Interactions of Surfactants with Polymers and Proteins. 1993;319 CRC Press, Boca Raton, FL.
26. Vermeer A.W.P., Norde W. Colloids Surf. A: Physicochem. Eng. Aspects. 161:2000;139.
27. Shastry M.C.R., Eftink M.R. Biochemistry. 35:1996;4094.
28. Rariy R.V., Bec N., Klyachko N.L., Levashov A.V. Biotechnol. Bioeng. 57:1998;552.
29. Galat A., Yang C.C., Boult E.R. Biochemistry. 24:1985;5678.
30. Kulig E., Wolny M. Int. J. Biochem. 20:(1):1988;79.
31. Hamada S., Takeda K. J. Protein Chem. 12:1993;477.
32. D'auria S., Barone R., Rossi M., Nucci R., Barone G., Fessas D., Bertoli E., Tanfani F. Biochem. J. 323:1997;833.
33. Zoungrana T., Findenegg G.H., Norde W. J. Colloid Interf. Sci. 190:(2):1997;437.
34. Vermeer A.W.P., Bermer M.G., Norde W. Biochim. Biophys. Acta. 1425:1998;1.
35. Prakash V., Nandi P.K., Jirgensons B. Int. J. Pept. Protein Res. 15:1980;305.
36. Pasta P., Carrca G., Longhi R., Zetta L. Biochim. Biophys. Acta. 1039:1990;1.
37. Gasset M., Onaderra M., Goormaghtigh E., Gavilancs J.G. Biochim. Biophys. Acta. 1080:1991;51.
38. Parker W., Song P.S. Biophys. J. 61:1992;1435.
39. Carpenter K.A., Schmidt R., Yue S.Y., Hodzic L., Pou C., Payza K., Godbout C., Brown W., Roberts E. Biochemistry. 38:1999;15295.
40. Park S.H., Kim Y.K., Park J.W., Lee B., Balny C., Lee B.J. Eur. J. Biochem. 267:2000;2695.
41. Bak M., Sorenson E.S., Rasmussen L.K., Sorensen O.W., Petersen T.E., Nielsen N.C. Eur. J. Biochem. 267:2000;188.
42. Manning M.C. Biochem. Biophys. Res. Commun. 160:1989;388.
43. Li S., Wang L.T., Zhou H.M. J. Protein Chem. 18:1999;653.
44. Moriyama Y., Ohta D., Kazuaki H., Mitsui Y., Takeda K. J. Protein Chem. 15:1996;265.
45. Hughson F.M., Wright P.E., Baldwin R.L. Science. 249:1990;1544.
46. Ptitsyn O.B., Pain R.H., Semisotnov G.V., Zerovnik E., Razgulyaev O.I. FEBS Lett. 262:1990;20.
47. Harding M.M., Williams D.H., Woolfson D.N. Biochemistry. 30:1991;3120.
48. Buck M., Radford S.E., Dobson C.M. Biochemistry. 32:1993;669.
49. Redfield C., Smith R.A.G., Dobson C.M. Nat. Struct. Biol. 1:1994;23-29.
50. Uversky V.N., Ptitsyn O.B. J. Mol. Biol. 255:1996;215.
51. Tatsumi E., Hirose M. J. Biochem. (Tokyo). 122:(2):1997;300.
52. Chaffotte A.F., Guijarro J.I., Guillou Y., Delepierre M., Goldberg M.E. J. Protein Chem. 16:1997;433.
53. Kuwajima K. Proteins: Struct. Funct. Genet. 6:1989;87.
54. Khurana R., Udgaonkar J.B. Biochemistry. 33:1994;106.
55. Edwin F., Jagannadham M.V. Arch. Biochem. Biophys. 381:2000;99.