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Dynamics of protein hydration by quasi-elastic neutron scattering


THE importance of water and its properties for biological systems makes the analysis of the dynamics of protein hydration of special interest1–3. It has long been recognised2 that neutron scattering can, in principle, provide the most complete description of molecular motions in hydrated biopolymers. Here we report the first results of an application of high-resolution quasi-elastic neutron scattering4–7 to the dynamics of protein hydration. A neutron beam incident on a biological sample produces scattered radiation that consists of a coherent part (that is, one that gives rise to an interference pattern which, in its Bragg scattering, contains the structural information8–10) and an incoherent part that cannot give interference effects but exhibits spectral changes which carry information on dynamic processes. Quasi-elastic neutron scattering explores the low-frequency region of the spectrum characterised by energy transfers of the order of, and less than, 1 cm−1. Because of the very large incoherent scattering cross-section of protons (80 b) relative to all other nuclei (<0.4 b) present in natural biological samples, the incoherent scattering is almost entirely due to hydrogenous groups and water molecules. By replacing some or all of the carbon-bound hydrogens by deuterium (2 b), dynamic contrast factors of up to 15 can be attained so that a wide range of contrast experiments becomes possible.

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RANDALL, J., MIDDENDORF, H., CRESPI, H. et al. Dynamics of protein hydration by quasi-elastic neutron scattering. Nature 276, 636–638 (1978).

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