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Optical Spectroscopic Techniques in High Pressure Bioscience

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High Pressure Molecular Science

Part of the book series: NATO Science Series ((NSSE,volume 358))

Abstract

High hydrostatic pressure induces changes in protein conformation, solvation and enzyme activities. To have access to these structural modifications, various biophysical techniques have been specially designed for high pressure experiments. Among them, spectroscopic methods are rather simple and easily adaptable both to high pressure and controlled temperatures. In the present paper, different improvements are presented together with some applications.

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References

  1. Mozhaev, V.V., Heremans, K., Frank, J., Masson, P. and Balny, C. (1996) High pressure effects on protein structure and function, Proteins: Struc. Func. Gen. 24, 81–91.

    Article  CAS  Google Scholar 

  2. Gross, M. and Jaenike, R. (1994) Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes, Eur. J. Biochem. 221, 617–630.

    Article  CAS  Google Scholar 

  3. Silva, J.L. and Weber, G. (1993) Pressure stability of proteins, Annu. Rev. Phys. Chem. 44, 89–113.

    Article  CAS  Google Scholar 

  4. Jonas, J. and Jonas, A. (1994) High-pressure NMR spectroscopy of proteins and membranes, Annu. Rev. Biophys. Biomol. Struct. 23, 287–318.

    Article  CAS  Google Scholar 

  5. Paladini, A.A. and Weber, G. (1981) Absolute measurements of fluorescence polarization at high pressures, Rev. Sci. Instr. 53, 419–427.

    Article  Google Scholar 

  6. Shimizu, T. (1992) High pressure experimental apparatus with windows for optical measurements up to 700 MPa, in C. Balny et al. (eds.), High Pressure and Biotechnology, Colloque INSERM/J. Libbey Eurotext, London, vol. 224, pp. 525–527.

    Google Scholar 

  7. Balny, C., Masson, P. and Travers, F. (1989) Some recent aspects of the use of high pressure for protein investigations in solution, High Press. Res. 2, 1–28.

    Article  Google Scholar 

  8. Douzou, P. (1977) Cryobiochemistry: an introduction, Academic Press, New York.

    Google Scholar 

  9. Hui Bon Hoa, G., Douzou, P., Dahan, N. and Balny, C. (1982) High pressure spectrophotometry at sub-zero temperatures, Anal. Biochem. 120, 125–135.

    Article  CAS  Google Scholar 

  10. Talsky, G. (1994) Derivative spectroscopy; low and high order, VCH, Weinheim.

    Google Scholar 

  11. Kornblatt, J.A., Kornblatt, M.J. and Hui Bon Hoa, G. (1995) Second derivative spectroscopy of enolase at high hydrostatic pressure: an approach to the study of macromolecular interactions, Biochemistry, 34, 1218–122

    Article  CAS  Google Scholar 

  12. Lange R., Frank, J., Saldana, J.-L. and Balny, C. (1996) Fourth derivative UV-spectroscopy of proteins under high pressure. I. Factors affecting the fourth derivative spectrum of the aromatic amino acids, Eur. Biophys. J. 24, 277–283.

    CAS  Google Scholar 

  13. Lange, R., Bec, N., Mozhaev, V.V. and Frank, J. (1996) Fourth derivative UV-spectroscopy of proteins under high pressure. II. Application to reversible structural changes, Eur. Biophys. J. 24, 284–292.

    CAS  Google Scholar 

  14. Balny, C., Saldana, J.-L., Lange, R., Kornblatt, M.J. and Kornblatt, J.A. (1996) UV/vis biochemical spectroscopy under high pressure, in P. R. von Rohr and Ch. Trepp (eds.), High Pressure Chemical Engineering, Elsevier Science, pp. 553–558.

    Google Scholar 

  15. Mombelli, E., Afshar, M., Fusi, P., Mariani, M., Tortora, P., Connelly, J.P. and Lange, R. (1997) The role of phenylalanine 31 in the maintaining the conformational stability of ribonuclease P2 from Sulfolobus solfataricus under extreme conditions of temperature and pressure, Biochemistry, 36, 8733–874

    Article  CAS  Google Scholar 

  16. Kunugi, S., Kitayaki, M., Yanagi, Y., Tanaka, N., Lange, R. and Balny, C. (1997) The effect of high pressure on thermolysin, Eur. J. Biochem. 248, 567–574.

    Article  CAS  Google Scholar 

  17. Kornblatt, M.J., Lange, R. and Balny, C. (1998) Can monomers of yeast enolase have enzymatic activity? Eur J. Biochem. 251, 775–780.

    Article  CAS  Google Scholar 

  18. Paladini, A.A. and Weber, G. (1981) Pressure-induced reversible dissociation of enolase, Biochemistry, 20, 2587–259

    Article  CAS  Google Scholar 

  19. Silva, J.L., Miles, E.W. and Weber, G. (1986) Pressure dissociation and conformational drift of the β dimer of tryptophan synthase, Biochemistry, 25, 5781–578

    Article  Google Scholar 

  20. Ruan, K. and Weber, G. (1989) Hysteresis and conformational drift of pressure-dissociated glyceraldehydephosphate dehydrogenase, Biochemistry, 28, 2144–215

    Article  CAS  Google Scholar 

  21. Royer, C.A., Hinck, A.P., Loh, S.N., Prehoda, K.E., Peng, X., Jonas, J. and Markley, J.L. (1993) Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as a monitired by fluorescence and nuclear magnetic resonance spectroscopy, Biochemistry, 32, 5222–523

    Article  CAS  Google Scholar 

  22. Harris, R.D., Jacobs, M., Long, M.M. and Urry, D.W. (1976) A high pressure sample cell for circular dichroism studies, Anal. Biochem., 73, 363–36

    Article  CAS  Google Scholar 

  23. Ozawa, S., Hayashi, R., Takahashi, S., Kawai, S. (1995) CD measurement of protein under high pressure in Abstracts, International Conference on High Pressure Bioscience and Biotechnology, Kyoto, A-3, p. 11.

    Google Scholar 

  24. Balny, C., Lange, R., Heitz, F., Connelly, J.P., Saldana, J.-L. and Ruan, K. (1998) High pressure as a tool to study protein conformation, Rev. High Pressure Sci. Technol. 7, 1292–1296.

    Article  CAS  Google Scholar 

  25. Markley, J.L., Travers, F. and Balny, C. (1981) Lack of evidence for a tetrahedral intermediate in the hydrolysis of nitroaniline substrates by serine proteinases, Eur. J. Biochem. 120, 477–485.

    Article  CAS  Google Scholar 

  26. Greiger R.A. and Eckert C.A. (1970) A new technique for chemical kinetics at high pressures AIChE J. 766–770

    Google Scholar 

  27. Sasaki, M., Amita, F. and Osugi, J. (1979) High pressure stopped-flow apparatus up to 3 kbar, Rev. Sci. Instr. 50 1104–1107.

    Article  CAS  Google Scholar 

  28. Smith, P. Beile, E. and Berger, R. (1982) An observation chamber for high-pressure stopped-flow apparatus, J. Biochem. Biophys. Methods, 6, 173–17

    Article  CAS  Google Scholar 

  29. Heremans, K., Snauwaert, J. and Rijkenberg, J. (1980) Stopped-flow apparatus for the study of fast reactions in solution under high pressure, Rev. Sci. Instr. 51, 806–808.

    Article  CAS  Google Scholar 

  30. Bugnon, P. Laurenczy, G. Ducommun, Y. Sauvageat, P.-Y., Merbach, E.A., Ith, R., Tschanz, R., Doludda, M. Bergbouer, R. and Grell, E. (1996) High-pressure stopped-flow spectrometer for kinetic studies of fast reactions by absorbance and fluorescence detection, Anal. Chem. 68, 3045–3049.

    Article  CAS  Google Scholar 

  31. Balny, C., Saldana, J.-L. and Dahan, N. (1984) High-pressure stopped-flow spectrometry at low temperatures, Anal. Biochem. 139, 178–189.

    Article  CAS  Google Scholar 

  32. Balny, C., Saldana, J.-L. and Dahan, N. (1987) High-pressure stopped-flow fluorometry at subzero temperatures: Application to kinetics of the binding of NADH to liver alcohol dehydrogenase, Anal Biochem. 163, 309–315.

    Article  CAS  Google Scholar 

  33. Takeda, N., Kato, M. and Taniguchi, Y. (1995) Pressure and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy, Biochemistry, 34, 5980–598

    Article  CAS  Google Scholar 

  34. Heremans, K., Rubens, P., Smeller, L., Vermeulen, G. and Goossens, K. (1996) Pressure versus temperature behaviour of proteins: FT-IR studies with the diamond anvil cell, in R. Hayashi and C. Balny (eds.), High Pressure Bioscience and Biotechnology, Elsevier Science, pp. 127–134.

    Google Scholar 

  35. Kato, M. and Taniguchi, Y. (1995) A hydrostatic optical cell with synthetic diamond windows for quantitative infrared measurements of fluids, Rev. Sci. Instrum. 66, 4333–4335.

    Article  CAS  Google Scholar 

  36. Reis, O., Winter, R. and Zerda, T.W. (1996) The effect of high external pressure on DPPC-cholesterol multilamellar vesicles. A pressure-tuning Fourier transform infrared spectroscopy, Biochim. Biophys. Acta, 1279, 5–1

    Article  Google Scholar 

  37. Geeves, M.A. (1991) The influence of pressure on actin and myosin interactions in solution and in single muscle fibres, J. Cell Sci., 14, 31–3

    CAS  Google Scholar 

  38. Davis, J.S. and Gutfreund, H. (1976) The scope of moderate pressure changes for kinetic and equilibrium studies of biochemical systems, FEBS Letters, 72, 199–20

    Article  CAS  Google Scholar 

  39. Bancel, F., Bec, N., Ebel, C. and Lange, R. (1997) A central role for water in the control of the spin state of cytochrome P-450scc, Eur. J. Biochem. 250, 276–285.

    Article  CAS  Google Scholar 

  40. Ruan, K., Lange, R., Zhou, Y. and Balny, C. (1998) Unusual affect of high hydrostatic pressure on basic phospholipase A2 from venom of Agkistrodon Halys Pallas, Biochem. Biophys. Res. Comm. 249, 844–8

    Article  CAS  Google Scholar 

  41. Luche, J.-L., Balny, C., Benefice, S., Denis, J.-M. and Petrier, C. (eds.) (1998) Chemical Processes and Reactions under Extreme or non-Classic Conditions, Off. Publ. Eur. Comm., Luxembourg.

    Google Scholar 

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Author information

Authors and Affiliations

  1. INSERM U 128, IFR 24, 1919, route de Mende, 34293, MONTPELLIER Cedex 5, France

    Claude Balny & Reinhard Lange

Authors
  1. Claude Balny
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  2. Reinhard Lange
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Editor information

Editors and Affiliations

  1. Department of Chemistry, Physical Chemistry, University of Dortmund, Dortmund, Germany

    Roland Winter

  2. School of Chemical Sciences, University of Illinois, Urbana, Illinois, USA

    Jiri Jonas

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© 1999 Springer Science+Business Media Dordrecht

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Balny, C., Lange, R. (1999). Optical Spectroscopic Techniques in High Pressure Bioscience. In: Winter, R., Jonas, J. (eds) High Pressure Molecular Science. NATO Science Series, vol 358. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4669-2_21

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  • DOI: https://doi.org/10.1007/978-94-011-4669-2_21

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-0-7923-5807-7

  • Online ISBN: 978-94-011-4669-2

  • eBook Packages: Springer Book Archive

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