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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This work has been funded by the German Federal Minister for Research and Technology (BMFT) under Contract No. 05 339 FBI5.
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Nienhaus, G.U., Hartmann, H., Parak, F. et al. Angular dependent rayleigh scattering of Mössbauer radiation on proteins. Hyperfine Interact 47, 299–310 (1989). https://doi.org/10.1007/BF02351614
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DOI: https://doi.org/10.1007/BF02351614