Proteins populate a multitude of states that interconvert on a broad range of timescales. To uncover how such dynamics contribute to protein function requires facing the experimental challenges associated with both the spatial complexity of proteins and the rapid timescales of potentially important motions. To overcome these issues, we combine methods of linear and two-dimensional infrared spectroscopy, with their inherent high temporal and spatial resolution, with chemical biology approaches for specific incorporation of vibrational reporter groups into proteins that provide frequency-resolved absorptions for characterizing their local environments.  We are applying this approach to measure residue-specific side chain dynamics of proteins toward evaluating their role in molecular recognition.

Residue-specific characterization of protein dynamics in molecular recognition via transparent window 1D/2D IR spectroscopy

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.