Paramasivam, Sivakumar2017-03-012017-03-012011http://udspace.udel.edu/handle/19716/20900Magic angle spinning (MAS) NMR spectroscopy has found applications as a versatile technique in chemistry and biochemistry to probe structure and dynamics of materials and biological systems. In recent years, MAS NMR spectroscopy has been rapidly developing as a method for atomic-resolution structural characterization of proteins and protein assemblies that are insoluble and difficult to crystallize. A number of laboratories including ours are working on developments of MAS technologies that would enable analysis of complex biological systems. In this dissertation, the applications of MAS NMR approaches to two types of problems in structural biology and biochemistry are demonstrated. First, structural and dynamics studies of two proteins, E. coli thioredoxin reassembly and dynein light chain 8 (DLC8) in the solid state are carried out yielding atomic-level details, as discussed in Chapters 2, 3, and 4. Second, ionization and tautomeric states of thiamin diphosphate cofactor (ThDP) in large protein, ThDP-dependent family of enzymes are probed using MAS NMR spectroscopy, described in Chapters 5 and 6.Nuclear magnetic resonance spectroscopy.Escherichia coli.Thioredoxin.Dynein.Ionization.TautomerismThiamin pyrophosphate.Enzymes.Thesis974008056