Membrane proteins have many important biological functions; however, their structures are difficult to be determined by conventional structural methods, including as solution NMR and X-ray crystallography under their native conditions. However, solid-state NMR can provide valuable structural information on membrane proteins, such as, chemical shift anisotropies and dipolar couplings, which can be used to solve the structures in phospholipid bilayer environments. Several membrane protein structures have been determined by mainly relying on 1H-15N dipolar couplings from amide backbone sites as measured in two-dimensional  separated-local-field experiments. In an effort to extend current methodologies, several new triple resonance (1H, 13C, and 15N) NMR experiments and signal processing methods are being developed. These include: 1. Measuring 1H-13C dipolar couplings in 13C uniformly labeled proteins for determining side-chain conformations. 2. Improving the efficiencies of 15N-13C magnetization transfer for 13C-detected 15N-13C correlation experiments. 3. Reducing the experimental time by non-uniform sampling and signal reconstructions. In initial results, the overall experiment efficiencies are increased by lmore than twenty fold, and a greater number of structural restraints are obtained as input for the protein structure calculations.

Solid-state NMR methodology development  for membrane proteins

243rd National Meeting (2012)

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