Structure And Function Of Bacteriorhodopsin Using Solid-state NMR

Membrane protein structure-function studies is a hot research area of today’s life sciences and pharmaceutical industry. Membrane protein plays a key role in the process of all life activities, and over60%drug action targets are membrane protein. Bacteriorhodopsin is a transmembrane protein that can act as an "energy switch" on the cell membrane of halophilic bacteria, it has a special proton pump function, which can convert light energy into chemical energy for the vital activities used. The structure of bacteriorhodopsin is similar with a number of important drug targets, such as GPCRs. Moreover, bacteriorhodopsin has a small molecular weight (26kDa), and it is easy to be prepared, thus it has become the ideal model protein for studying transmembrane protein. Solid-state NMR technique was developed in recent years,it is a very sensitive mean which can reach the atomic resolution level for obtaining protein structural information.Solid-state NMR methods contained chemical shifts assignments,one-dimensional NMR experiments and multidimensional NMR experiments etc.The first step in protein NMR studies is to prepare stable isotope labeling protein.Solid-state NMR technique can study the protein of natural conformation, it is a very effective and forefront mean in membrane protein structure-function studies.This article firstly collated, summarized and analyzed the reported bacteriorhodopsin solid-state NMR data. Subsequently, the paper analyzed the the growth of halophilic bacteria and the biosynthesis of bacteriorhodopsinin in synthetic medium. Finally, I made some literature research about the metabolism of Halobacterium and discussed the feasible labeling strategies of bacteriorhodopsin.