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首页> 外文期刊>Biochemistry >Characterization of the Hydrodynamic Properties of the Folding Transition State of an SH3 Domain by Magnetization Transfer NMR Spectroscopy
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Characterization of the Hydrodynamic Properties of the Folding Transition State of an SH3 Domain by Magnetization Transfer NMR Spectroscopy

机译：磁化转移NMR光谱表征SH3域折叠过渡态的流体力学性质

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Protein folding kinetic data have been obtained for the marginally stable N-terminal Src homology 3 domain of the Drosophila protein drk (drkN SH3) in an investigation of the hydrodynamic properties of its folding transition state.Due to the presence of NMR resonances of both folded and unfolded states at equilibrium,kinetic data can be derived from NMR magnetization transfer techniques under equilibrium conditions.Kinetic analysis as a function of urea (less than approx 1 M) and glycerol enables determination of a values,measures of the energetic sensitivity of the transition state to the perturbation relative to the end states of the protein folding reaction (the folded and unfolded states).Both end states have previously been studied experimentally by NMR spectroscopic and other biophysical methods in great detail and under nondenaturing conditions.Combining these results with the kinetic folding data obtained here,we can characterize the folding transition state without requiring empirical models for the unfolded state structure.We are thus able to give a reliable measure of the solvent-accessible surface area of the transition state of the drkN SH3 domain (4730 +- 360 A~2) based on urea titration data.Glycerol titration data give similar results and additionally demonstrate that folding of this SH3 domain is dependent on solvent viscosity,which is indicative of at least partial hydration of the transition state.Because SH3 domains appear to fold by a common folding mechanism,the data presented here provide valuable insight into the transition states of the drkN and other SH3 domains.
机译：通过研究果蝇蛋白质drk（drkN SH3）的边缘过渡态的流体动力学特性，获得了果蝇蛋白质drk（drkN SH3）的边缘稳定的N端Src同源性3结构域的蛋白质折叠动力学数据。平衡状态下的未折叠状态，动力学数据可从平衡条件下的NMR磁化传递技术中得出。动力学分析作为尿素（小于约1 M）和甘油的函数，可以确定一个值，并测量跃迁的能量敏感性相对于蛋白质折叠反应的最终状态（折叠和未折叠状态）的微扰状态，先前已经通过NMR光谱法和其他生物物理方法在非变性条件下进行了详细的实验研究，研究了两种最终状态。此处获得的动力学折叠数据，我们无需弯折就可以表征折叠转变状态因此，我们可以根据尿素滴定数据对drkN SH3域（4730 +-360 A〜2）过渡态的溶剂可及表面积进行可靠的测量。数据给出相似的结果，并进一步证明此SH3结构域的折叠取决于溶剂粘度，这表明过渡态至少有部分水合。由于SH3结构域似乎是通过常见的折叠机制折叠的，因此本文提供的数据提供了有价值的信息。深入了解drkN和其他SH3域的过渡状态。

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