Monitoring the effects of strong cosolvent hexafluoroisopropanol in investigation of the tetrameric structure and stability of K+-channel KcsA

Archives of Biochemistry and Biophysics

Volumn 498, Issue 1, 2010, Pages 1-6

  Raja, Mobeen ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

Author keywords

Circular dichroism; Hexafluoroisopropanol; Membrane lateral pressure; Potassium channel KcsA; Protein lipid interaction; Tetrameric stability; Tryptophan fluorescence

Indexed keywords

HEXAFLUORO 2 PROPANOL; MEMBRANE LIPID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLGLYCEROL; POTASSIUM CHANNEL; POTASSIUM CHANNEL KCSA; TRYPTOPHAN; UNCLASSIFIED DRUG;

ADSORPTION; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; HYDROGEN BOND; HYDROPHOBICITY; LIPID BILAYER; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

BACTERIAL PROTEINS; MODELS, MOLECULAR; POTASSIUM CHANNELS, VOLTAGE-GATED; PROPANOLS; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SEQUENCE DELETION; SOLVENTS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

EID: 77952952247     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2010.03.014     Document Type: Article

References (32)

1. Ullrich A., Schlessinger J. Cell 1990, 61:203-212.
2. Metzger H. J. Immunol. 1992, 149:1477-1487.
3. Goodsell D.S., Olson A.J. Annu. Rev. Biophys. Biomol. Struct. 2000, 29:105-153.
4. Ali M.H., Imperiali B. Bioorg. Med. Chem. 2005, 13:5013-5020.
5. Popot J.L., Engelman D.M. Biochemistry 1990, 29:4031-4037.
6. Popot J.L., Engelman D.M. Annu. Rev. Biochem. 2000, 69:881-922.
7. Stowell M.H.B., Rees D.C. Adv. Protein Chem. 1995, 46:279-311.
8. Otzen D.E., Nesgaard L. Biochemistry 2007, 46:4348-4359.
9. Dyson H.J., Wright P.E. Curr. Opin. Struct. Biol. 1993, 3:60-65.
10. Yang J.J., Buck M., Pitkeathly M., Kotik M., Haynie D.T., Dobson C.M., Radford S.E. J. Mol. Biol. 1995, 252:483-491.
11. Hiroto N., Mizuno K., Goto Y. Protein Sci. 1997, 6:416-421.
12. Wood S.J., Maleeff B., Hart T., Wetzel R. J. Mol. Biol. 1996, 256:870-877.
13. Zhang H., Kaneko K., Nguyen J.T., Livshits T.L., Baldwin M.A., Cohen F.E., James T.L., Prusiner S.B. J. Mol. Biol. 1995, 250:514-526.
14. Valiyaveetil F.I., Zhou Y., MacKinnon R. Biochemistry 2002, 41:10771-10777.
15. Cortes D.M., Perozo E. Biochemistry 1997, 36:10343-10352.
16. Van Dalen A., Hegger S., Killian J.A., de Kruijff B. FEBS Lett. 2002, 525:33-38.
17. Raja M., Spelbrink R.E.J., de Kruijff B., Killian J.A. FEBS Lett. 2007, 581:5715-5722.
18. van den Brink-van der Laan E., Chupin V., Killian J.A., de Kruijff B. Biochemistry 2004, 43:5937-5942.
19. van den Brink-van der Laan E., Chupin V., Killian J.A., de Kruijff B. Biochemistry 2004, 43:4240-4250.
20. Raja M. J. Membr. Biol. 2010, 234:235-240.
21. Raja M.M., Tyagi N.K., Kinne R.K.H. J. Biol. Chem. 2003, 278:49154-49163.
22. Barrera F.N., Renart M.L., Molina M.L., Poveda J.A., Encinar J.A., Fernandez A.M., Neira J.L., Gonzalez-Ros J.M. Biochemistry 2005, 44:14344-14352.
23. Doyle D.A., Morais C.J., Pfuetzner R.A., Kuo A., Gulbis J.M., Cohen S.L., Chait B.T., MacKinnon R. Science 1998, 280:69-77.
24. Cantor R.S. Toxicol. Lett. 1998, 100:451-458.
25. Patra M., Salonen E., Terama E., Vattulainen I., Faller R., Lee B., Holopainen J., Karttunen M. Biophys. J. 2006, 90:1121-1135.
26. Chin J.H., Goldstein D.B. Mol. Pharmacol. 1977, 13:435-441.
27. Komatsu H., Okada S. Chem. Phys. Lipids 1997, 85:67-74.
28. Chen S.Y., Yang B., Jacobson K., Sulik K.K. Alcohol 1996, 13:589-595.
29. Kamatari Y.O., Konno T., Kataoka M., Akasaka K. J. Mol. Biol. 1996, 259:512-523.
30. Peoples R.W., Li C., Weight F.F. Annu. Rev. Pharmacol. Toxicol. 1996, 36:185-201.
31. Miller K.W. Br. J. Anaesth. 2002, 89:17-31.
32. Mascia M.P., Trudell J.R., Harris R.A. Proc. Natl. Acad. Sci. USA 2000, 97:9305-9310.