“Linking time-resolved crystallography to dynamics and allosteric processes in proteins”

​

This project explores protein dynamics by combining room-temperature serial crystallography with advanced modeling techniques to capture alternative conformations. Using time-resolved crystallography, the study will visualize structural motions in NQO1 and Fascin proteins, both of which exhibit allosteric regulation. A combination of ligand mixing and solvent-based temperature jump strategies will trigger conformational changes, revealing how atomic vibrations evolve into functionally relevant structural fluctuations. Additionally, inhibitor binding will be used to assess how key motions contribute to enzyme activity. The findings will establish temperature-jump as a universal tool for studying protein dynamics, providing broader insights into enzyme catalysis and allosteric regulation.

​

Reference: CNS2022-135713

​

Participating Institutions: CSIC
 

Start and End dates: 09/01/2023 - 31/08/2025
 

PI: José M. Martín García
 

Funding Agency: