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- W1989383119 abstract "Modern biophysics has benefited greatly from the use of X-ray and neutron diffraction from ordered single crystals of proteins and other macromolecules to give highly detailed pictures of these molecules in the solid state. However, the most biologically relevant environments for these molecules are liquid solutions, and their liquid state properties are sensitive to details of the liquid structuring. The best experimental method for studying such structuring is also neutron diffraction, but of course, the inherent disorder of the liquid state means that these experiments cannot hope to achieve the level of informational detail available from single crystal diffraction. Nonetheless, recent advances in neutron beam intensity, beam stability, and detector sensitivity mean that it should be possible, at least in principle, to use such measurements to extract information about structuring in much more complex systems than have previously been studied. We describe a series of neutron diffraction studies of isotopically labeled molecules in aqueous solution which, when combined with results from computer simulations, can be used to extract conformational information of the hydration of the molecules themselves, essentially opening up new avenues of investigation in structural biology." @default.
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- W1989383119 date "2010-12-23" @default.
- W1989383119 modified "2023-09-27" @default.
- W1989383119 title "Simulation and Neutron Diffraction Studies of Small Biomolecules in Water" @default.
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- W1989383119 doi "https://doi.org/10.1007/s11483-010-9192-x" @default.
- W1989383119 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3171504" @default.
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