title: Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.
abstract: Paramagnetism-based nuclear pseudocontact shifts and spin relaxation enhancements contain a wealth of information in solid-state NMR spectra about electron-nucleus distances on the ∼20 Å length scale, far beyond that normally probed through measurements of nuclear dipolar couplings. Such data are especially vital in the context of structural studies of proteins and other biological molecules that suffer from a sparse number of experimentally-accessible atomic distances constraining their three-dimensional fold or intermolecular interactions. This perspective provides a brief overview of the recent developments and applications of paramagnetic magic-angle spinning NMR to biological systems, with primary focus on the investigations of metalloproteins and natively diamagnetic proteins modified with covalent paramagnetic tags.
authors: Department of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA. Electronic address: jaroniec@chemistry.ohio-state.edu.
authors: Christopher P
authors: CP
authors: Jaroniec
mesh_terms: D000465:Algorithms; D060526:Magnetic Fields; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D011506:Proteins
keywords: Magic-angle spinning; Paramagnetic relaxation enhancement; Protein structure; Pseudocontact shift; Solid-state NMR