Abstract
The physical properties of the neutron makes it an ideal tool to investigate the structure and dynamics of macromolecules. For biological systems, neutrons can probe motions that range from protein internal dynamics to global motions of proteins in solutions or in cells. Both types of studies can bring specific information on the way the macromolecules realize their function, at the single molecule level or collectively. We review how the different types of motion can be separated and which kind of approach is the more suited for a specific study. The coupling between internal dynamics and protein function has been the center of a large number of studies which are often controversial. We define the theoretical concepts and critically review some experimental and numerical results. On a larger lengthscale, protein diffusion in solution can be compared to the theories developed for the investigation of colloids dynamics, which can aid the interpretations of diffusion measurements in cells.
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Longeville, S., Doster, W. (2012). Protein Dynamics and Function. In: García Sakai, V., Alba-Simionesco, C., Chen, SH. (eds) Dynamics of Soft Matter. Neutron Scattering Applications and Techniques. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-0727-0_8
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