Physics of Proteins at Low Temperature

Springer Science and Business Media LLC - Tập 137 - Trang 289-317 - 2004
Vladimir V. Ponkratov1, Josef Friedrich1, Jane M. Vanderkooi2, Alexander L. Burin3, Yuri A. Berlin4
1Physics Department E14 and Lehrstuhl für Physik Weihenstephan, Technische Universität München, D-853350 Freising, Germany
2Department of Biochemistry and Biophysics, USA
3Department of Chemistry, Tulane University, New Orleans, USA
4Department of Chemistry, Northwestern University, USA

Tóm tắt

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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