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Cold Denaturation of Proteins Under Pressure Studied by Time-Resolved Fluorescence. Application to Ribonuclease P2 from S. sofataricus

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Advances in High Pressure Bioscience and Biotechnology

Abstract

The ribonuclease P2 and the F31A one point mutation form of the hydrophobic core of the enzyme have been studied in term of heterogenity of conformational states. A cold denaturation under pressure of the F31A mutant takes place below 0 °C since the wild-type form is more resistant and changes are quite reversible.

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Author information

Authors and Affiliations

  1. LBPA, Ecole Normale Supérieure de Cachan, IGR, CNRS UMR1772, Cachan, France

    P. Tauc & J. C. Brochon

  2. Universita degli di Milano, via Celoria 26, 20133, Milano, Italy

    P. Fusi & P. Tortora

  3. INSERM U128, BP5051, 34033, Montpellier, France

    R. Lange

Authors
  1. P. Tauc
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  2. P. Fusi
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  3. P. Tortora
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  4. R. Lange
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  5. J. C. Brochon
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Editor information

Editors and Affiliations

  1. Section Physical Chemistry, University of Heidelberg, Institute for Pharmaceutical Technology and Biopharmacy, Im Neuenheimer Feld 346, D -69120, Heidelberg, Germany

    Horst Ludwig

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© 1999 Springer-Verlag Berlin Heidelberg

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Tauc, P., Fusi, P., Tortora, P., Lange, R., Brochon, J.C. (1999). Cold Denaturation of Proteins Under Pressure Studied by Time-Resolved Fluorescence. Application to Ribonuclease P2 from S. sofataricus . In: Ludwig, H. (eds) Advances in High Pressure Bioscience and Biotechnology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60196-5_41

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  • DOI: https://doi.org/10.1007/978-3-642-60196-5_41

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-64300-2

  • Online ISBN: 978-3-642-60196-5

  • eBook Packages: Springer Book Archive

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