Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.
Protein Sci. 2013 Oct;22(10):1313-9. doi: 10.1002/pro.2318. Epub 2013 Aug 20.
Intrinsic rates of exchange are essential parameters for obtaining protein stabilities from amide (1) H exchange data. To understand the influence of the intracellular environment on stability, one must know the effect of the cytoplasm on these rates. We probed exchange rates in buffer and in Escherichia coli lysates for the dynamic loop in the small globular protein chymotrypsin inhibitor 2 using a modified form of the nuclear magnetic resonance experiment, SOLEXSY. No significant changes were observed, even in 100 g dry weight L(-1) lysate. Our results suggest that intrinsic rates from studies conducted in buffers are applicable to studies conducted under cellular conditions.
固有交换率是从酰胺（1）H 交换数据中获得蛋白质稳定性的重要参数。为了了解细胞内环境对稳定性的影响，必须了解细胞质对这些速率的影响。我们使用改良的核磁共振实验 SOLEXSY，探测了在缓冲液中和大肠杆菌裂解物中小球状蛋白胰凝乳蛋白酶抑制剂 2 的动态环的交换速率。即使在 100 g 干重 L(-1)的裂解物中，也没有观察到明显的变化。我们的结果表明，在缓冲液中进行的研究中的固有速率可适用于细胞条件下进行的研究。
