Abstract
High-pressure biochemistry started to emerge in the 1960s and 1970s and focused on the effects of pressure on proteins, nucleoproteins and membranes. During the same time, NMR spectroscopy was combined with high pressure since it is the only generally applicable method to monitor pressure-induced structural changes at the atomic level in solution. However, up to now the application of many, if not most, of the currently available multidimensional high-resolution NMR experiments is impossible under high pressure in protein solutions due to the restricted volume of the high-pressure glass cells, which causes a poor signal–to–noise ratio. In addition, a prerequisite for the understanding of pressure effects on proteins is the knowledge about the dependence on 1H chemical shifts in random coil model tetrapeptides and buffer systems. Furthermore, we review various high-pressure NMR experiments on proteins and the recent advances made in this field.
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