title: Magic angle spinning solid-state NMR experiments for structural characterization of proteins.
abstract: Solid-state nuclear magnetic resonance (SSNMR) has become a prominent method in biology and is suitable for the characterization of insoluble proteins and protein aggregates such as amyloid fibrils, membrane-lipid complexes, and precipitated proteins. Often, the initial and the most critical step is to obtain spectroscopic assignments, that is, to determine chemical shifts of individual atoms. The procedures for SSNMR spectroscopic assignments are now well established for small microcrystalline proteins, where high signal-to-noise can be obtained. The sensitivity of the experiments and spectral resolution decrease with the increasing molecular weight, which makes setting SSNMR experiments in large proteins a much more challenging and demanding procedure. Here, we describe the protocol for the most common set of 3D magic angle spinning (MAS) SSNMR experiments. While the procedures described in the text are well known to SSNMR practitioners, we hope they will be of interest to scientists interested in extending their repertoire of biophysical techniques.
authors: Department of Physics and Biophysical Interdepartmental Group, University of Guelph, Guelph, ON, Canada.
authors: Lichi
authors: L
authors: Shi
authors: Vladimir
authors: V
authors: Ladizhansky
mesh_terms: D000218:Adamantane / Q000737:chemistry; D000465:Algorithms; D002138:Calibration; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012243:Rhodopsin / Q000737:chemistry*; D025604:Rhodopsins, Microbial / Q000737:chemistry*
chemical_list: D025604:Rhodopsins, Microbial; C413548:proteorhodopsin; D012243:Rhodopsin; D000218:Adamantane