Photoswitching of terahertz structural dynamics in the photosynthesis photoprotector orange carotenoid protein

Abstract

Computational studies have shown picosecond protein structural dynamics enable efficient conformational transitions during biological function. These structural dynamics necessarily change with each conformational change, providing overall steering throughout the functional cycle. Here we examine the switching of these long range collective structural vibrations of the photosynthesis protein orange carotenoid protein using anisotropic terahertz microspectroscopy, which provides dynamical fingerprinting for biomacromolecules by using polarization sensitive measurements of aligned samples, as provided by protein crystals.