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Determination of partial molal volumes, and salt and water binding, of highly charged biological macromolecules (tRNA, halophilic protein) in multimolar salt solutions

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Book cover Analytical Ultracentrifugation V

Part of the book series: Progress in Colloid and Polymer Science ((PROGCOLLOID,volume 113))

Abstract

Highly charged macromolecules such as nucleic acids or halophilic proteins cannot be considered without their environment of ions and water. Density, equilibrium sedimentation and neutron scattering were used to characterize yeast tRNAphe in high concentrations of NaCl or MgCl2 and halophilic malate dehydrogenase from Haloarcula marismortui in high-concentration NaCl solutions. Methods were compared and used in a complementary way to determine partial molal volumes and solvent binding parameters, which, when the hypothesis of an invariant particle is valid, provide solvation values for the macromolecule.

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Authors and Affiliations

  1. CEA-CNRS, Institut de Biologie Structurale, 41 avenue des martyrs, F-38027, Grenoble Cedex 1, France

    B. Kernel, G. Zaccai & C. Ebel

Authors
  1. B. Kernel
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  2. G. Zaccai
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  3. C. Ebel
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Corresponding author

Correspondence to C. Ebel .

Editor information

Helmut Cölfen

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© 1999 Springer-Verlag

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Kernel, B., Zaccai, G., Ebel, C. (1999). Determination of partial molal volumes, and salt and water binding, of highly charged biological macromolecules (tRNA, halophilic protein) in multimolar salt solutions. In: Cölfen, H. (eds) Analytical Ultracentrifugation V. Progress in Colloid and Polymer Science, vol 113. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-48703-4_24

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  • DOI: https://doi.org/10.1007/3-540-48703-4_24

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  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-66175-7

  • Online ISBN: 978-3-540-48703-6

  • eBook Packages: Springer Book Archive

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