Effect of lipids on the thermal stability and conformational changes of proteins: Ribonuclease A and cytochrome c

International Journal of Pharmaceutics

Volumn 161, Issue 2, 1998, Pages 137-148

  Lo, Yu Li ^a   Rahman, Yueh Erh ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Cytochrome c; Differential scanning calorimetry; Dipalmitoylphosphatidylglycerol; Fourier transform infrared spectroscopy; Ribonuclease A

Indexed keywords

CYTOCHROME C; DIPALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLGLYCEROL; RIBONUCLEASE A;

ARTICLE; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; DRUG STABILITY; ENTHALPY; HYDROGEN BOND; IN VITRO STUDY; INFRARED SPECTROSCOPY; MODEL; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE; SURFACE CHARGE; THERMOSTABILITY;

EID: 0032559540     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-5173(97)00344-X     Document Type: Article

References (32)

1. Arrondo J.L.R., Muga A., Castresana J., Goni F.M. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59:1993;23-56.
2. Battistel E., Bianchi D., Rialdi G. Thermodynamics of immobilized ribonuclease A. Pure Appl. Chem. 63:1991;1483-1490.
3. Blackburn, P., Moore, S., 1982. Pancreatic Ribonuclease. In: Boyer, P.D. (Ed.), The Enzymes. Academic Press, New York, pp. 317-433.
4. Byler D.M., Susi H. Examination of the secondary structure on proteins by deconvoluted FTIR spectra. Biopolymers. 25:1986;469-487.
5. Chen P.S., Toribara T.Y., Warner H. Microdetermination of phosphorus. Anal. Chem. 28:1956;1756-1758.
6. Dikerson R.E., Takano T., Eisenberg D., Kallai O.B., Samson L., Cooper A., Margoliash E. Ferricytochrome c. J. Biol. Chem. 246:1971;1511-1535.
7. Dousseau F., Pezolet M. Determination of the secondry structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods. Biochemistry. 29:1990;8771-8779.
8. Fabian H., Schultz C., Naumann D., Landt O., Hahn U., Saenger W. Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. A Fourier transform infrared spectroscopic study. J. Mol. Biol. 232:1993;967-981.
9. 2O demonstrates that collagen monomers undergo a conformational transition prior to thermal self-assembly in vitro. Biochemistry. 30:1991;2372-2377.
10. Heimburg T., Marsh D. Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: An FTIR study. Biophys. J. 65:1993;2406-2417.
11. Hildebrandt P., Heimburg T., Marsh D. Quantitative conformational analysis of cytochrome c bound to phospholipid vesicles studied by resonance Raman spectroscopy. Eur. Biophys. J. 18:1990;193-201.
12. Kartha G., Bello J., Harker D. Tertiary structure of ribonuclease. Nature. 213:1967;862-865.
13. LaBrake C.C., Wang L., Keiderling T.A., Fung L.W.M. Fourier transform infrared spectroscopic studies of the secondary structure of spectrin under different ionic strengths. Biochemistry. 32:1993;10296-10302.
14. Lepock J.R., Ritchie K.P., Kolios M.C., Rodahl A.M., Heinz K.A., Krunv J. Influence of transiton rates and scan rate on kinetic simulations of differential scannig calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry. 31:1992;12706-12712.
15. Levitt M., Greer J. Automatic identification of secondary structure in globular proteins. J. Mol. Biol. 114:1977;181-239.
16. Manavaian P., Johnson W.C. Jr. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167:1987;76-85.
17. Margoliash E., Schejter A. Cytochrome c. Adv. Protein Chem. 21:1966;113-286.
18. Muga A., Mantsch H.H., Surewicz W.K. Membrane binding induces destabilization of cytochrome c structure. Biochemistry. 30:1991;7219-7224.
19. Privalov P.L. Stability of proteins. Small globular proteins. Adv. Protein Chem. 33:1979;167-241.
20. Privalov P.L. Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35:1982;1-104.
21. Privalov P.L., Khechinashvili N.N. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J. Mol. Biol. 86:1974;665-684.
22. Richards, F.M., Wyckoff, H.W., 1971. Bovine pancreatic ribonuclease. In: Boyer, P.D. (Ed.), The Enzymes. Academic Press, New York, pp. 649-806.
23. 1H-NMR evaluation of the ferricytochrome c-cardiolipin interaction. Effect of superoxide radicals. Biochem. J. 265:1990;227-232.
24. Straume M., Freire E. Two-dimensional differential scanning of calorimetry: Simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis. Anal. Chem. 203:1992;259-268.
25. Sturtevant J.M. Some applications of calorimetry in biochemistry and biology. Annu. Rev. Biophys. Bioeng. 3:1974;35-51.
26. Sturtevant J.M. Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38:1987;463-488.
27. Surewicz W.W., Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta. 952:1988;115-130.
28. Van Wart H.E., Scheraga H.A. Raman and resonance Raman spectroscopy. Methods Enzymol. 49:1978;67-149.
29. Vanderkooi, J., Erecinska, M., 1976. Cytochrome c, a membrane-bound enzyme. In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes. Plenum, New York, 1976, pp. 43-86.
30. Zhang Y.-P., Lewis R.N.A.H., Hodges R.S., McElhaney R.N. FIIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane α-helices of membrane proteins. Biochemistry. 31:1992;11572-11578.
31. Zhang Y.-P., Lewis R.N.A.H., Hodges R.S., McElhaney R.N. Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies. Biochemistry. 31:1992;11579-11588.
32. Zhang Y.-P., Lewis R.N.A.H., Hodges R.S., McElhaney R.N. Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylethanolamine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies. Biophys. J. 68:1995;847-857.