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Physics of Proteins at Low Temperature

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Abstract

We present results of a hole burning study with thermal cycling and waiting time spectral diffusion experiments on a modified cytochrome - c protein in its native as well as in its denatured state. The experiments show features which seem to be characteristic for the protein state of matter and its associated dynamics at low temperature. The properties responsible for the observed patterns are organisation paired with randomness and, in addition, the finite size which gives rise to surface and solvent effects. We discuss some general model approaches which might serve as guide lines for understanding these features.

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Authors and Affiliations

  1. Physics Department E14 and Lehrstuhl für Physik Weihenstephan, Technische Universität München, D-853350 Freising, Germany

    Vladimir V. Ponkratov & Josef Friedrich

  2. Department of Biochemistry and Biophysics, Philadelphia, PA 19104, USA

    Jane M. Vanderkooi

  3. Department of Chemistry, Tulane University, New Orleans, LA 70118, USA

    Alexander L. Burin

  4. Department of Chemistry, Northwestern University, IL 60208, USA

    Yuri A. Berlin

Authors
  1. Vladimir V. Ponkratov
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  2. Josef Friedrich
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  3. Jane M. Vanderkooi
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  4. Alexander L. Burin
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  5. Yuri A. Berlin
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Ponkratov, V.V., Friedrich, J., Vanderkooi, J.M. et al. Physics of Proteins at Low Temperature. Journal of Low Temperature Physics 137, 289–317 (2004). https://doi.org/10.1023/B:JOLT.0000049058.81275.72

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  • DOI: https://doi.org/10.1023/B:JOLT.0000049058.81275.72

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