Raw NMR data for "Production of Bacteriorhodopsin for NMR Structural Studies"

Abstract Since its discovery in 1971, bacteriorhodopsin from Halobacterium salinarum has become one of the most extensively characterized membrane proteins. Nevertheless, significant gaps remain in our understanding of its functional mechanism. From a structural biology perspective, the molecular basis for the transitions between different states upon light absorption is still unclear. NMR spectroscopy offers unique capabilities to elucidate these dynamic processes. In this study, we present optimized protocols for bacteriorhodopsin sample preparation, evaluate various membrane mimetics, and demonstrate that bicelles represent a perfect environment for NMR-based investigations of this protein's structure and dynamics. The present dataset contains NMR Raw Fids data used in the article, prepared for publication