Large-scale oscillatory motions in myoglobin

Abstract

Elastic and inelastic components of neutron scattering from lyophilized myoglobin were measured at wavevector transfers, Q of 1.0, 1.4, 1.85, and 3.0 Å^-1 and at temperatures of 77 and 298 K. The elastic scattering determines an overall effective mean square atomic displacement which was employed in a simple harmonic Langevin formalism to obtain effective force constants describing molecular deformations. These force constants and the inelastic data are compatible with alpha helices as a vibrating species at room temperature, and with amino acid residues as the vibrating entities at 77 K. The present measurements are consistent with recent molecular dynamics calculations.