The use of NMR spectroscopy to study the structures and dynamics of membrane systems is described. The principal nuclei used are 1H, 2H, 13C and 31P. Both oriented and nonoriented systems can be investigated. In addition, peptides and proteins embedded in membranes can be studied.

How molecules convert light energy to perform a specific transformation is a fundamental question in photophysics. Ultrafast spectroscopy reveals the kinetics associated with electronic energy flow, but little is known about how absorbed photon energy drives nuclear motion. Here we used ultrabroadband transient absorption spectroscopy to monitor coherent vibrational energy flow after photoexcitation of the retinal chromophore. In the proton pump bacteriorhodopsin, we observed coherent activation of hydrogen-out-of-plane wagging and backbone torsional modes that were replaced by unreactive coordinates in the solution environment, concomitant with a deactivation of the reactive relaxation pathway.