Abstract
The flexibility of protein molecules reveals itself in several experiments. X-ray structure analysis of protein crystals shows that the unit cells are not identical. Different molecules have slightly different structures called conformational substates. The derivation of molecules from their average structure as determined by the x-ray method can be measured by the mean square displacement, 〈x 2〉x, which can be obtained for each atom of the molecule. Displacement of the atoms can be caused by thermal vibrations. However, since x-ray diffraction of single crystals is a coherent effect of all unit cells static disorder in the molecules contributes also to 〈x 2〉x. No information on the time scale of motions contributing to the 〈x 2〉x-values can be obtained from x-ray structure analysis.
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Parak, F., Hartmann, H., Nienhaus, G. (1987). The Mössbauer Effect as a Probe of Protein Dynamics. In: Austin, R., et al. Protein Structure. Proceedings in Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4796-8_6
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DOI: https://doi.org/10.1007/978-1-4612-4796-8_6
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