A protein’s ‘dance steps’ affect its biological function

Abstract

A new microspectroscopy technique can track changes in the directions of complex protein vibrations. The method could enable researchers to determine how an enzyme responds when an inhibitor binds to it, for instance, or when the enzyme develops a mutation. At the ACS national meeting in San Francisco on April 4, physicist Andrea G. Markelz of the University at Buffalo, SUNY, reported that by using her group’s technique, anisotropic terahertz microscopy, she found that a protein can undergo large changes in “global vibrations,” which resemble intricate protein dance steps, even though the protein vibrational energy hardly changes (Biophys. J. 2017, DOI: 10.1016/j.bpj.2016.12.049). Researchers had assumed that biologically relevant changes in global vibrations would be accompanied by obvious changes in a protein’s vibrational energy states. But until now, scientists have been limited to measuring energy state distributions, and studies have shown that those didn’t really change. So researchers concluded th...