Hyperfine Interactions

, Volume 47, Issue 1–4, pp 299–310 | Cite as

Angular dependent rayleigh scattering of Mössbauer radiation on proteins

  • G. U. Nienhaus
  • H. Hartmann
  • F. Parak
  • J. Heinzl
  • E. Huenges
Oral Contributions

Abstract

RSMR experiments with57Fe radiation were performed on myoglobin. An areasensitive detector was employed for simultaneous angular dependent collection of the scattered quanta up to a maximum angle 2θ of 17‡. Experimental data of polycrystalline and lyophilized myoglobin are compared with computer calculations of the scattering which are based on the atomic coordinates determined by X-ray structure analysis. Special attention has been paid to the influence of coherence effects from collectively moving parts of the protein. A simple model is introduced in order to take into account these segmental motions. Our first results indicate that the sizes of collectively moving segments are comparable with spheres of about 6 å in diameter in dry myoglobin. In myoglobin crystals, where the molecules are surrounded by large hydration shells, the movements appear to be correlated in segments with sizes comparable to helices.

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Copyright information

© J.C. Baltzer AG, Scientific Publishing Company 1989

Authors and Affiliations

  • G. U. Nienhaus
    • 1
  • H. Hartmann
    • 1
  • F. Parak
    • 1
  • J. Heinzl
    • 2
  • E. Huenges
    • 2
  1. 1.Institut für Physikalische Chemie der UniversitÄt MünsterMünsterF.R.G.
  2. 2.Physik-Department der T.U. MünchenGarchingF.R.G.

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