title: High-resolution nuclear magnetic resonance studies of proteins.
abstract: The combination of advanced high-resolution nuclear magnetic resonance (NMR) techniques with high-pressure capability represents a powerful experimental tool in studies of protein folding. This review is organized as follows: after a general introduction of high-pressure, high-resolution NMR spectroscopy of proteins, the experimental part deals with instrumentation. The main section of the review is devoted to NMR studies of reversible pressure unfolding of proteins with special emphasis on pressure-assisted cold denaturation and the detection of folding intermediates. Recent studies investigating local perturbations in proteins and the experiments following the effects of point mutations on pressure stability of proteins are also discussed. Ribonuclease A, lysozyme, ubiquitin, apomyoglobin, alpha-lactalbumin and troponin C were the model proteins investigated.
authors: Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana, Urbana, IL 61801, USA. j-jonas@uiuc.edu
authors: Jiri
authors: J
authors: Jonas
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D017510:Protein Folding; D011506:Proteins / Q000032:analysis*
chemical_list: D011506:Proteins