Protein Dynamics by Two-Dimensional Infrared Spectroscopy
Overview
Affiliations
Proteins function as ensembles of interconverting structures. The motions span from picosecond bond rotations to millisecond and longer subunit displacements. Characterization of functional dynamics on all spatial and temporal scales remains challenging experimentally. Two-dimensional infrared spectroscopy (2D IR) is maturing as a powerful approach for investigating proteins and their dynamics. We outline the advantages of IR spectroscopy, describe 2D IR and the information it provides, and introduce vibrational groups for protein analysis. We highlight example studies that illustrate the power and versatility of 2D IR for characterizing protein dynamics and conclude with a brief discussion of the outlook for biomolecular 2D IR.
Singh S, Gyawali Y, Jiang T, Bukowski G, Zheng H, Zhang H J Biol Inorg Chem. 2024; 29(2):243-250.
PMID: 38580821 PMC: 11181464. DOI: 10.1007/s00775-024-02046-0.
Biomolecular infrared spectroscopy: making time for dynamics.
Hunt N Chem Sci. 2024; 15(2):414-430.
PMID: 38179520 PMC: 10763549. DOI: 10.1039/d3sc05223k.
Increasing Pump-Probe Signal toward Asymptotic Limits.
Robben K, Cheatum C J Phys Chem B. 2023; 127(21):4694-4707.
PMID: 37200488 PMC: 10240498. DOI: 10.1021/acs.jpcb.3c01270.