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首页> 外文期刊>Journal of Molecular Biology >The Cold Denatured State Is Compact but Expands at Low Temperatures: Hydrodynamic Properties of the Cold Denatured State of the C-terminal Domain of L9.
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The Cold Denatured State Is Compact but Expands at Low Temperatures: Hydrodynamic Properties of the Cold Denatured State of the C-terminal Domain of L9.

机译：冷变性状态是致密的，但在低温下会膨胀：L9 C端结构域的冷变性状态的流体力学性质。

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摘要

A point mutation of a small globular protein, the C-terminal domain of L9 destabilizes the protein and leads to observable cold-denaturation at temperatures above zero. The cold denatured state is in slow exchange with the native state on the NMR time scale, and this allows the hydrodynamic properties of the cold unfolded state and the native state to be measured under identical conditions using pulsed-field gradient NMR diffusion measurements. This provides the first experimental measurement of the hydrodynamic properties of a cold unfolded protein and its folded form under identical conditions. Hydrodynamic radii of the cold-induced unfolded states were measured for a set of temperatures ranging from 2 degrees C to 25 degrees C at pD 6.6 in the absence of denaturant. The cold unfolded state is compact compared to the urea or acid unfolded state and a trend of increasing radii of hydration is observed as the temperature is lowered. These observations are confirmed by experiments on the same protein atpD 8.0, where it is more stable, in the presence of a modest concentration of urea. The expansion of the cold-denatured state at lower temperatures is consistent with the temperature dependence of hydrophobic interactions.
机译：小球状蛋白的点突变，L9的C末端结构域使蛋白不稳定，并在高于零的温度下导致可观察到的冷变性。冷变性状态在NMR时间尺度上与原始状态缓慢交换，这使得可以使用脉冲场梯度NMR扩散测量在相同条件下测量冷未折叠状态和原始状态的流体力学性质。这提供了在相同条件下冷未折叠蛋白及其折叠形式的流体动力学特性的首次实验测量。在不存在变性剂的情况下，在pD 6.6下测量了一组温度范围为2摄氏度至25摄氏度的冷诱导未折叠状态的流体力学半径。与尿素或酸的未折叠状态相比，冷的未折叠状态是致密的，并且随着温度降低，观察到水合半径增加的趋势。这些观察结果通过在中等浓度尿素存在下对相同蛋白atpD 8.0的实验进行了证实，该蛋白更稳定。低温下冷变性状态的膨胀与疏水相互作用的温度依赖性一致。

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