X-ray Study on Protein Dynamics

Abstract

Proteins must fluctuate to perform cellular functions, such as enzymatic catalysis, protein-protein interactions, and interactions with DNA and RNA. The time scale of protein dynamics is typically ranging from ps to ms, requiring various techniques to cover different time regimes. In this presentation, we will first explain some of the latest X-ray techniques to study protein dynamics. Those will include time-resolved small angle X-ray scattering, diffuse scattering analysis, temperature-controlled X-ray crystallography, cryo-trapping X-ray crystallography, and fs pump-probe serial crystallography. Afterwards, we will describe the experimental results on human carbonic anhydrase II (hCA II), revealing the restoration mechanism of the proton transfer solvent network during hCA II catalysis.