Hyperfine Interactions

, Volume 47, Issue 1, pp 299–310

Angular dependent rayleigh scattering of Mössbauer radiation on proteins

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

DOI: 10.1007/BF02351614

Cite this article as:
Nienhaus, G.U., Hartmann, H., Parak, F. et al. Hyperfine Interact (1989) 47: 299. doi:10.1007/BF02351614

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.

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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