Raw NMR data for "Bicelles as a prospective membrane mimetics for NMR Structural Studies of Bacteriorhodopsins"

Abstract of the manuscript: 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 different isotopic labeling combined with a bicelle environment represents a prospective approach for NMR-based investigations of this protein's structure and dynamics. Description of the dataset: The present dataset contains NMR Raw FIDs in the Bruker format. These NMR Raw FIDs were used in the manuscript (Figure 2), prepared for publication.