High-hydrostatic pressure is an alternative perturbation method that can be used to destabilize globular proteins. Generally perfectly reversible, pressure exerts local effects on regions or domains of a protein containing internal voids, contrary to heat or chemical denaturant that destabilize protein structures uniformly. When combined with NMR spectroscopy, high pressure (HP) allows one to monitor at a residue-level resolution the structural transitions occurring upon unfolding and to determine the kinetic properties of the process. The use of HP-NMR has long been hampered by technical difficulties. Owing to the recent development of commercially available high-pressure sample cells, HP-NMR experiments can now be routinely performed. This review summarizes recent advances of HP-NMR techniques for the characterization at a quasi-atomic resolution of the protein folding energy landscape.

中文翻译：

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高压扰动与核磁共振波谱相结合，用于蛋白质折叠途径的结构和动力学表征


高静水压是另一种扰动方法，可用于破坏球状蛋白质的稳定性。通常完全可逆，压力对含有内部空隙的蛋白质的区域或结构域产生局部影响，这与均匀破坏蛋白质结构稳定的热或化学变性剂相反。当与核磁共振波谱相结合时，高压 (HP) 允许人们以残基水平分辨率监测展开时发生的结构转变，并确定该过程的动力学特性。 HP-NMR 的使用长期以来一直受到技术困难的阻碍。由于最近市售高压样品池的发展，HP-NMR 实验现在可以常规进行。本综述总结了 HP-NMR 技术的最新进展，用于以准原子分辨率表征蛋白质折叠能量景观。