Study of the photocycle of the metastable states of SRII and their mutants with the use of light activated NMR spectroscopy

TL;DR

This study investigates the photo cycle of SRII and its mutants using light-activated NMR spectroscopy to understand conformational changes and key structural states involved in its function.

Contribution

It introduces the use of light-activated NMR spectroscopy to analyze the metastable states of SRII and its mutants, revealing structural insights into its photo cycle.

Findings

Identification of metastable states in SRII's photocycle

Structural characterization of key residues involved

Insights into the mechanism of SRII function

Abstract

Sensory rhodopsin II (SRII) is a seven helix protein that belongs to the rhodopsin protein family. Light induced conformational changes govern SRII's function. These changes are related to the photo cycle of the protein that is comprised of various metastable states. After the completion of this cycle the protein returns to its ground state. Mutational studies of key residues will reveal the mechanism that underlies the function of the protein. The result will allow us to determine key structures at various PHs involved in the photo cycle of SRII and to understand the protein's function and mechanism.