Liquid-like Side-chain Dynamics in Myoglobin

Abstract : At temperatures above ∼200 K the motions of atoms in globular proteins contain a non-vibrational component that gives rise to characteristic elastic and quasi-elastic neutron scattering profiles. There is evidence that the non-vibrational dynamic is required for protein function. Here we show by analysing a molecular dynamics simulation of myoglobin that the neutron scattering results from liquid-like rigid-body motion of the protein side-chains.
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Gérald Kneller, Jeremy Smith. Liquid-like Side-chain Dynamics in Myoglobin. Journal of Molecular Biology, Elsevier, 1994, 242 (3), pp.181-185. ⟨10.1006/jmbi.1994.1570⟩. ⟨hal-02156653⟩

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