Structure and dynamics of proteins by high-resolution solid-state NMR
Résumé
Solid-state NMR spectroscopy has significantly grown in recent years, and is rapidly becoming a powerful structural tool in chemistry and biology. Steadily ongoing methodological developments combined with tremendous engineering advances in probe and spectrometer hardware, along with notably increased magnetic field strengths, have paved the way for studying the structure and dynamics of solid chemical and biological samples at atomic resolution spanning a broad atlas of structures ranging from materials to protein aggregates or membrane proteins. This communication presents an outline of this experimental technique, of its recent progress, and of its immense potential. As a case study, the structural and dynamical determination of a paramagnetic human enzyme, the Cu(II),Zn(II)-superoxide dismutase, in microcrystalline form will be presented.