Abstract
Advanced high-resolution NMR spectroscopy, including 2D NMR techniques, combined with the high-pressure capability represents a powerful new tool in studies of proteins. Selected results taken from recent studies illustrate the high information content and the range of problems that can be investigated. Design features and performance characteristics of high-sensitivity, high-resolution, variable-temperature NMR probes operating at 500 MHz and at pressures up to 900 MPa are described. The main portion of this chapter deals with an overview of several recent studies or studies in progress from our laboratory using 1D and 2D high-resolution, high-pressure NMR spectroscopy to investigate the pressure-induced reversible unfolding and cold denaturation of proteins. The following proteins were studied: ribonuclease A, lysozyme, apomyoglobin, arc repressor, and ubiquitin.
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Ballard, L., Jonas, J. (2002). High-Pressure NMR Spectroscopy of Proteins. In: Taniguchi, Y., Stanley, H.E., Ludwig, H. (eds) Biological Systems Under Extreme Conditions. Biological and Medical Physics Series. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-04802-3_4
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DOI: https://doi.org/10.1007/978-3-662-04802-3_4
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