How soft is a protein? A protein dynamics force constant measured by neutron scattering

Abstract

An effective environmental force constant is introduced to quantify the molecular resilience (or its opposite, "softness") of a protein structure and relate it to biological function and activity. Specific resilience-function relations were found in neutron-scattering experiments on purple membranes containing bacteriorhodopsin, the light-activated proton pump of halobacteria; the connection between resilience and stability is illustrated by a study of myoglobin in different environments. Important advantages of the neutron method are that it can characterize the dynamics of any type of biological sample-which need not be crystalline or monodisperse-and that it enables researchers to focus on the dynamics of specific parts of a complex structure with deuterium labeling.