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Structural Distributions, Fluctuations and Conformational Changes in Proteins Investigated by Mössbauer Spectroscopy and X-Ray Structure Analysis

  • Fritz Parak
Part of the Progress in Mathematics book series (NSSA)

Abstract

This contribution shows how X-ray structure analysis and Mössbauer spectroscopy can be used as complementary methods in the investigation of protein dynamics. X-ray analysis measures structural distributions via mean square displacements without having any time resolution. Mössbauer spectroscopy on 57Fe labels dynamics on a time scale faster 100 ns. Even in the extrapolation to T = 0 K myoglobin has no well defined structure with one energy minimum. The molecules are in different conformational substates. At physiological temperatures the structural distribution in the liganded (or unliganded) conformation is larger than the structural differences between these conformations. Fluctuations through conformational substates and changes of the conformation are highly correlated. The structure distribution around the heme iron influences the oxygen binding.

Fluctuations in myoglobin envolve diffusion-like segmental motions in a restricted space. The characteristic size of the segments is about 5 A. Drying of the sample or freezing of the hydration water reduces these fluctuations drastically. The Brownian type motion of segments can also be found in membranes.

Keywords

Wave Train Heme Iron Structural Distribution M6ssbauer Spectrum Heme Pocket 
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

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Fritz Parak
    • 1
  1. 1.Institut für Physikalische Chemie der UniversitätMünsterFederal Republic of Germany

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