Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
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DOI：
10.1002/anie.201509168
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发表时间：
2015-12-14
期刊：
影响因子：
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通讯作者：
Lewandowski JR
中科院分区：
文献类型：
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作者：
Lamley JM;Öster C;Stevens RA;Lewandowski JR
了解相互作用蛋白质的动力学是描述许多生物物理过程的关键一步。在这里，我们调查的骨干动力学蛋白GB 1在两个不同的组件：晶体GB 1和沉淀GB 1-抗体复合物的分子量超过300 kDa。 我们对含有低至8纳摩尔GB 1的样品进行这些测量。 通过测量特定位置的15 N弛豫速率（包括弛豫色散），我们获得了在时间尺度上跨越9个数量级的动态快照。 在两种环境中对GB 1的测量结果进行比较表明，虽然蛋白质的许多动态特征在它们之间是保守的（特别是对于快速的皮秒-纳秒运动），但对于慢运动发生更大的差异，其中>500 ns范围内的运动在复合物中更普遍。 数据表明，GB 1可能会经历一个小振幅的整体各向异性运动采样复杂的相互作用界面。
Understanding the dynamics of interacting proteins is a crucial step toward describing many biophysical processes. Here we investigate the backbone dynamics for protein GB1 in two different assemblies: crystalline GB1 and the precipitated GB1–antibody complex with a molecular weight of more than 300 kDa. We perform these measurements on samples containing as little as eight nanomoles of GB1. From measurements of site‐specific 15N relaxation rates including relaxation dispersion we obtain snapshots of dynamics spanning nine orders of magnitude in terms of the time scale. A comparison of measurements for GB1 in either environment reveals that while many of the dynamic features of the protein are conserved between them (in particular for the fast picosecond–nanosecond motions), much greater differences occur for slow motions with motions in the >500 ns range being more prevalent in the complex. The data suggest that GB1 can potentially undergo a small‐amplitude overall anisotropic motion sampling the interaction interface in the complex.