Recent Advances in Magic‐Angle Spinning Solid‐State NMR of Proteins

Abstract

Magic‐angle spinning (MAS) solid‐state NMR (SSNMR) spectroscopy is emerging as an important technique for the determination of three‐dimensional structures of biological molecules and for the characterization of their dynamics. While there is an established suite of MAS SSNMR experiments for protein structure determination in small‐ and medium‐sized proteins, these methods face many challenges in large systems. In this review, recent progress in MAS NMR spectroscopy is discussed, specifically focusing on the emerging developments aimed at improving the sensitivity and resolution of SSNMR that are likely to determine its future applications. These developments include sample preparation and isotopic labeling strategies, fast MAS, proton detection, and paramagnetic NMR spectroscopy.

NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins

“…Membrane proteins are also extremely appealing targets for SSNMR since the growth of single crystals for X-ray diffraction experiments is challenging [4][5][6][63][64][65]. SSNMR can access these systems in microcrystalline form as well as in their native lipid environment.…”

The NMR–Rosetta capsid model of M13 bacteriophage reveals a quadrupled hydrophobic packing epitope

“…That is, a fivefold rotation of the major coat protein subunit around the virion axis (pentamers) and an approximate 36°rotation relating two successive pentamers [in fd-Y21M a precise 36°rotation was reported; for fd, values of −33.23°(18) and −34.62° (22) were reported]. All studies report that the coat protein is mostly right-handed, curved, α-helical, with a flexible or disordered N terminus.Magic-angle spinning (MAS) solid-state NMR has become a popular tool for studying the structure and dynamics of biological molecules (25)(26)(27). The method can be implemented on a variety of systems from small peptides to macromolecular biological assemblies.…”

“…Magic-angle spinning (MAS) solid-state NMR has become a popular tool for studying the structure and dynamics of biological molecules (25)(26)(27). The method can be implemented on a variety of systems from small peptides to macromolecular biological assemblies.…”

Magic-angle spinning NMR of intact bacteriophages: Insights into the capsid, DNA and their interface

“…Site-specific resonance assignment is therefore key to understanding phage properties. Many pulse sequences aimed at chemical shift assignments have been developed and are based on the acquisition of multi-dimensional experiments involving well established dipolar-based and J-based correlations of 1 H, 15 N and 13 C nuclei [33,[56][57][58][59]. 13 as well as sidechain assignment.…”

“…It is well established that magic-angle spinning (MAS) solid-state NMR (ssNMR) provides high-quality data on structure and dynamics for high-molecular weight intact biocomplexes in native-like states [33][34][35][36]. Clearly, MAS ssNMR has advantages over other techniques to study bacteriophage systems, as it does not require crystallinity, alignment or cryogenic treatment.…”