title: New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy.
abstract: In the past several decades solution NMR spectroscopy has emerged as a powerful technique for the study of the structure and dynamics of proteins, providing detailed insights into biomolecular function. Herein, I provide a summary of two important areas of application, focusing on NMR studies of (i) supramolecular systems with aggregate molecular masses in the hundreds of kilodaltons and of (ii) sparsely populated and transiently formed protein states that are thermally accessible from populated ground-state conformers. The critical role of molecular dynamics in function is emphasized, highlighting the utility of the NMR technique in providing such often elusive information.
authors.affiliation: Departments of Molecular Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, ON, Canada M5S 1A8; Hospital for Sick Children, Program in Molecular Structure and Function, 555 University Avenue, Toronto, ON, Canada M5G 1X8.
authors.forename: Lewis E
authors.initials: LE
authors.lastname: Kay
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D012996:Solutions
chemical_list: D011506:Proteins; D012996:Solutions
keywords: conformational studies; functional dynamics; proteasome; solution NMR spectroscopy