Solid-State Deuterium NMR Spectroscopy of Membranes

Solid-state NMR spectroscopy is widely applicable to the investigation of non-crystalline or amorphous materials, e.g. polymers, glasses, protein precipitates, and membrane proteins. Rather than being mainly an alternative to X-ray crystallography, solid-state NMR is virtually unique among current analytical and spectroscopic methodologies in that it provides both structural and dynamical information at an atomically resolved level. In solid-state NMR, the structural information is obtained from the static or motionally averaged coupling tensors due to dipolar, chemical shift, or quadrupolar interactions [1,2]. Corresponding dynamical information is acquired from the tensor fluctuations, which depend on the mean-squared amplitudes and rates of the motions and affect the NMR lineshapes and relaxation times. For these reasons, solid-state NMR is finding increasing applicability in the chemistry of materials, structural biology, and genomics research, and this trend can be expected to continue well into the future.