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Hyperfine Interactions

, Volume 40, Issue 1–4, pp 147–157 | Cite as

Protein structural dynamics as determined by Mössbauer spectroscopy

  • Fritz Parak
  • Joachim Heidemeier
  • Gerd U. Nienhaus
Invited Papers, Concluding Remarks

Abstract

Mössbauer spectroscopy on57Fe allows the study of dynamics with a characteristic time faster 100 ns. For myoglobin a detailed physical picture of protein dynamics has been obtained. A myoglobin molecule has no well defined energy minimum. X-ray structure analysis yields only an average conformation. At low temperatures the molecules are trapped in slightly different structures called conformational substates. At higher temperatures a Brownian type of oscillation of molecular segments in restricted space occurs. RSMR technique allows an estimation of the characteristic size of these segments which are in myoglobin well below 30 A and larger than 6 A. A determination of the quasielastic absorption with high accuracy yields the energy distribution of the conformational substates. As further examples bacteriorhodopsin and a model compound for membranes are discussed.

Keywords

Thin Film Structure Analysis Energy Minimum Energy Distribution Characteristic Time 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© J.C. Baltzer AG, Scientific Publishing Company 1988

Authors and Affiliations

  • Fritz Parak
    • 1
  • Joachim Heidemeier
    • 1
  • Gerd U. Nienhaus
    • 1
  1. 1.Institut für Physikalische Chemie der UniversitätMünsterFed. Rep. of Germany

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