Structural and dynamic studies of proteins by high-resolution solid-state NMR

Solid-state NMR (SSNMR) spectroscopy provides unique possibilities for the structural investigation of insoluble or non-crystalline molecules (e.g., membrane proteins) at the atomic level. Recent efforts aim at solving the complete structures of biological macromolecules using high-resolution magic-angle spinning NMR. Structurally homogenous samples of [C-13, N-15]-labeled proteins are used in this type of studies. Sequential correlation of resonances, detection of tertiary inter-atomic contacts and characterization of torsion angles can be achieved using multidimensional homo- and heteronuclear correlation experiments. This review discusses the recent progress made in resonances assignments, structure and dynamics determination, as well as the detection of protein interaction partners by SSNMR methods.