title: High-resolution, high-pressure NMR studies of proteins.
abstract: Advanced high-resolution NMR spectroscopy, including two-dimensional NMR techniques, combined with high pressure capability, represents a powerful new tool in the study of proteins. This contribution is organized in the following way. First, the specialized instrumentation needed for high-pressure NMR experiments is discussed, with specific emphasis on the design features and performance characteristics of a high-sensitivity, high-resolution, variable-temperature NMR probe operating at 500 MHz and at pressures of up to 500 MPa. An overview of several recent studies using 1D and 2D high-resolution, high-pressure NMR spectroscopy to investigate the pressure-induced reversible unfolding and pressure-assisted cold denaturation of lysozyme, ribonuclease A, and ubiquitin is presented. Specifically, the relationship between the residual secondary structure of pressure-assisted, cold-denatured states and the structure of early folding intermediates is discussed.
authors.affiliation: Beckman Institute for Advanced Science and Technology, School of Chemical Sciences, University of Illinois, Urbana, Illinois 61801, USA. J.-Jonas@uiuc.edu
authors.forename: J
authors.initials: J
authors.lastname: Jonas
authors.forename: L
authors.initials: L
authors.lastname: Ballard
authors.forename: D
authors.initials: D
authors.lastname: Nash
mesh_terms: D055592:Biophysical Phenomena; D001703:Biophysics; D003080:Cold Temperature; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy / Q000295:instrumentation / Q000379:methods*; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry; D011312:Pressure; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D013696:Temperature; D014452:Ubiquitins / Q000737:chemistry
chemical_list: D011506:Proteins; D014452:Ubiquitins; D012259:Ribonuclease, Pancreatic; D009113:Muramidase