European Biophysics Journal

, Volume 29, Issue 2, pp 146–152 | Cite as

Nuclear forward scattering of synchrotron radiation by deoxymyoglobin

  • C. Keppler
  • K. Achterhold
  • A. Ostermann
  • U. van Bürck
  • A. I. Chumakov
  • R. Rüffer
  • W. Sturhahn
  • E. E. Alp
  • F. G. Parak
BIOPHYSICS LETTER

Abstract

Nuclear forward scattering of synchrotron radiation is used to determine the quadrupole splitting and the mean square displacement of the iron atom in deoxymyoglobin in the temperature range between 50 K and 243 K. Above 200 K an abnormally fast decay of the forward scattered intensity at short times after the synchrotron flash is observed, which is caused by protein-specific motions. The results strongly support the picture that protein dynamics seen at the position of the iron can be understood by harmonic motions in the low temperature regime while in the physiological regime diffusive motions in limited space are present. The shape of the resonance broadening function is investigated. An inhomogeneous broadening with a Lorentzian distribution indicating dipole interactions results in a better agreement with the experimental data than the common Gaussian distribution.

Key words Myoglobin Protein dynamics Nuclear forward scattering Mössbauer effect Synchrotron radiation 

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Copyright information

© Springer-Verlag Berlin Heidelberg 2000

Authors and Affiliations

  • C. Keppler
    • 1
  • K. Achterhold
    • 1
  • A. Ostermann
    • 1
  • U. van Bürck
    • 2
  • A. I. Chumakov
    • 3
  • R. Rüffer
    • 3
  • W. Sturhahn
    • 4
  • E. E. Alp
    • 4
  • F. G. Parak
    • 1
  1. 1.Fakultät für Physik E17, Technische Universität München, 85747 Garching, GermanyDE
  2. 2.Fakultät für Physik E15, Technische Universität München, 85747 Garching, GermanyDE
  3. 3.European Synchrotron Radiation Facility, BP 220, 38043 Grenoble Cedex, FranceFR
  4. 4.Advanced Photon Source, Argonne National Laboratory, Argonne, IL 60439, USAUS

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