Correlated motions in proteins arising from the collective movements of residues have long been proposed to be fundamentally important to key properties of proteins, from catalysis and allostery to evolvability. Recent breakthroughs in structural biology have made it possible to capture proteins undergoing complex conformational changes, yet the subtle and intrinsic fluctuations within a single conformation remain one of the least understood facets of protein structure. For many decades, the analysis of diffuse X-ray scattering held the promise of animating crystal structures with such correlated motions. With recent advances in both X-ray detectors, this long-held promise can now be met. In this talk, I’ll describe our recent work in interpreting this signal and discuss how it can be used to the understand the role of correlated motions in enzymes.
Support or Funding Information
NIH F32 fellowship GM117757 to SPM, NIH grants GM100008 (to NA), GM124847 (to NA), and GM122086 (to DAC), and by start-up funds from Princeton University and Cornell University to NA.
The three-dimensional diffuse scattering map contains information about correlated protein motions.
