LIQUID-LIKE SIDE-CHAIN DYNAMICS IN MYOGLOBIN

At temperatures above similar to 200 K the motions of atoms in globula r proteins contain a non-vibrational component that gives rise to char acteristic elastic and quasi-elastic neutron scattering profiles. Ther e is evidence that the non-vibrational dynamics is required for protei n function. Here we show by analysing a molecular dynamics simulation of myoglobin that the neutron scattering results from liquid-like rigi d-body motion of the protein side-chains.