PubMed · 8089839
Liquid-like side-chain dynamics in myoglobin.
Abstract
At temperatures above approximately 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 dynamics 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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G R Kneller, J C Smith. 1994-09-23. Liquid-like side-chain dynamics in myoglobin.. https://doi.org/10.1006/jmbi.1994.1570
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