title: Protein structure determination by magic-angle spinning solid-state NMR, and insights into the formation, structure, and stability of amyloid fibrils.
abstract: Protein structure determination methods using magic-angle spinning solid-state nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable development in the past decade. Significant advances in instrumentation, sample preparation, spectroscopic techniques, and computational methods have made possible the determination of the first high-resolution structures of a peptide and a protein in 2002. Subsequent developments allowed the investigation of larger proteins, the initial application of automated analysis routines, and substantial improvements in structural resolution. The application of these methods has enabled the investigation of amyloid fibril structures, conformational dynamics, and their assembly pathways at an atomic level for the first time, as these are systems not accessible by other common techniques. Recent advances and future trends for protein structure determination using MAS SSNMR, as well as its application to the study of amyloid fibrils, are reviewed.
authors.affiliation: Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA. gcomell2@illinois.edu
authors.forename: Gemma
authors.initials: G
authors.lastname: Comellas
authors.forename: Chad M
authors.initials: CM
authors.lastname: Rienstra
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D055550:Protein Stability
chemical_list: D000682:Amyloid; D010455:Peptides