High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins
High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins
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DOI：
10.1016/j.ymeth.2004.03.010
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发表时间：
2004-09-01
期刊：
影响因子：
4.8
通讯作者：
Akasaka, K
中科院分区：
文献类型：
--
作者：
Kamatari, YO;Kitahara, R;Akasaka, K
最近使用高压核磁共振波谱对蛋白质进行了广泛的结构研究，这可能有助于我们了解蛋白质折叠机制。压力将构象平衡从较高体积的构象体转移到较低体积的构象体。如果压力发生变化，从折叠的天然结构开始，在许多情况下，我们会在完全展开之前观察到中间构象异构体。这使得能够研究平衡条件下蛋白质各种中间构象异构体的结构和热力学特征的细节。我们还可以检查压力对一些典型变性状态（例如螺旋变性、熔球和展开状态）的结构和稳定性的影响。高压核磁共振方法还可用于研究寡聚或聚集蛋白的缔合/解离平衡。除了直接观察压力跃变时的动力学中间体之外，压力下平衡构象异构体的 NMR 结构研究还提供了有关折叠/解折叠反应期间动力学中间体结构的信息。 (C) 2004 年，爱思唯尔公司出版。
Extensive structural studies using high-pressure NMR spectroscopy have recently been carried out on proteins, which potentially contribute to our understanding of the mechanisms of protein folding. Pressure shifts the conformational equilibrium from higher to lower volume conformers. If the pressure is varied, starting from the folded native structure, in many cases we observe intermediate conformers before the onset of total unfolding. This enables the investigation of details of the structure and thermodynamic characteristics of various intermediate conformers of proteins under equilibrium conditions. We can also examine pressure effects on the structure and stability of some typical denatured states such as helical denatured, molten globule, and unfolded states. The high-pressure NMR method can also be used to investigate association/dissociation equilibria of oligomeric or aggregated proteins. Beside direct observation of kinetic intermediates upon pressure jump, NMR structural investigations of equilibrium conformers under pressure provide information about the structures of kinetic intermediates during folding/unfolding reactions. (C) 2004 Published by Elsevier Inc.