Magic‐Angle Spinning Solid‐State Nuclear Magnetic Resonance: Application to Structural Biology

Abstract The application of magic‐angle spinning (MAS) solid‐state NMR methods to large‐scale problems in structural biology has seen a significant progress in the last decade. Improved hardware, better sample preparation techniques, and new methodologies have resulted in the ability to solve the three‐dimensional structures of proteins, and to study their dynamic properties, making this method a viable and important tool for understanding the relation between biological processes and protein structure and function. One of the biggest advantages of MAS solid‐state NMR is in the ability to study structures, which are not easily accessible by traditional methods such as X‐ray crystallography and solution NMR. Hence, new classes of important proteins and biological complexes such as membrane proteins, amyloid fibrils and prions, metalloenzymes, and viruses, have all been characterized to various extents. It is expected that the role of MAS solid‐state NMR in structural biology will increase significantly as the number of dedicated research groups rises, and methodologies and hardware further improve.