Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography.

ABSTRACT: The vast majority of protein structures are determined at cryogenic temperatures, which are far from physiological conditions. Nevertheless, it is well established that temperature is an essential thermodynamic parameter for understanding the conformational dynamics and functionality of proteins in their native environments. Time-resolved crystallography is a technique that aims to elucidate protein function by examining structural alterations during processes such as ligand binding, catalysis, or allostery. However, this approach is typically conducted under ambient conditions, which may obscure crucial conformational states, that are only visible at physiological temperatures. In this study, we directly address the interplay between protein structure and activity via a method that enable

SUBMITTER: Schulz EC 

PROVIDER: S-EPMC12267849 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature