Abstract
During the years since the first Brookhaven Symposium of this kind, the scope of neutron spectroscopy has broadened considerably as the result of increased flux levels and advances in instrumentation, implemented primarily at the Institut Laue-Langevin in Grenoble. The potential of high resolution neutron spectroscopy as applied to the study of protein-water and protein-ligand dynamics is due to a unique combination of three factors:
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a)
the wide range of hydrogen/deuterium contrast conditions that can be created in a binary or ternary scattering system involving partially or fully deuterated proteins;
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b)
the frequency region covered by neutron techniques (106 to 1013 Hz), bridging the nanosecond to picosecond gap where data are lacking, as well as providing sufficient overlap with complementary information derived from other techniques;
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c)
the fact that the small energy differences characteristic of weakly interacting molecular systems are resolved along with spatial information in the 1 to 100-Å region.
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Middendorf, H.D., Randall, J.T., Crespi, H.L. (1984). Neutron Spectroscopy of Hydrogenous and Biosynthetically Deuterated Proteins. In: Schoenborn, B.P. (eds) Neutrons in Biology. Basic Life Sciences, vol 27. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0375-4_23
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DOI: https://doi.org/10.1007/978-1-4899-0375-4_23
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