Hyperfine Interactions

, Volume 40, Issue 1, pp 147–157

Protein structural dynamics as determined by Mössbauer spectroscopy

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

DOI: 10.1007/BF02049086

Cite this article as:
Parak, F., Heidemeier, J. & Nienhaus, G.U. Hyperfine Interact (1988) 40: 147. doi:10.1007/BF02049086

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.

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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