Analysis of Sub-τc and Supra-τc Motions in Protein Gβ1 Using Molecular Dynamics Simulations
Analysis of Sub-τc and Supra-τc Motions in Protein Gβ1 Using Molecular Dynamics Simulations
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DOI：
10.1016/j.bpj.2009.07.061
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发表时间：
2009-11-04
影响因子：
3.4
通讯作者：
Dobson, Christopher M.
中科院分区：
文献类型：
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作者：
Bui, Jennifer M.;Gsponer, Joerg;Dobson, Christopher M.
蛋白质的功能依赖于其天然状态在广泛时间尺度上的动力学行为。为了研究这些动态的情况下，小蛋白G β 1，我们分析了分子动力学模拟与无模型方法的核磁弛豫。我们发现了与从自旋弛豫测量获得的S-2一致的快速时间尺度运动的振幅（子τ（c），其中τ（c）是旋转相关时间），以及与从残余偶极耦合测量获得的S-2阶参数定量一致的慢速时间尺度运动的振幅（超τ（c））。缓慢的时间尺度运动与（3）J耦合的大变化有关，这些耦合是在不同构象子态之间发生转变之后发生的。这些结果提供了进一步表征的大的结构波动的天然状态的蛋白质，发生在时间尺度上长于旋转相关时间。
The functions of proteins depend on the dynamical behavior of their native states on a wide range of timescales. To investigate these dynamics in the case of the small protein G beta 1, we analyzed molecular dynamics simulations with the modelfree approach of nuclear magnetic relaxation. We found amplitudes of fast timescale motions (sub-tau(c), where tau(c) is the rotational correlation time) consistent with S-2 obtained from spin relaxation measurements as well as amplitudes of slow timescale motions (supra-tau(c)) in quantitative agreement with S-2 order parameters derived from residual dipolar coupling measurements. The slow timescale motions are associated with the large variations of the (3)J couplings that follow transitions between different conformational substates. These results provide further characterization of the large structural fluctuations in the native states of proteins that occur on timescales longer than the rotational correlation time.