Institute of Natural Sciences and Department of Physics and Astronomy, Shanghai Jiao Tong University, Shanghai 200240, China.
Department of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Sci Adv. 2016 Oct 14;2(10):e1600886. doi: 10.1126/sciadv.1600886. eCollection 2016 Oct.
Protein function often depends on global, collective internal motions. However, the simultaneous quantitative experimental determination of the forms, amplitudes, and time scales of these motions has remained elusive. We demonstrate that a complete description of these large-scale dynamic modes can be obtained using coherent neutron-scattering experiments on perdeuterated samples. With this approach, a microscopic relationship between the structure, dynamics, and function in a protein, cytochrome P450cam, is established. The approach developed here should be of general applicability to protein systems.
蛋白质的功能通常依赖于整体的、集体的内部运动。然而，这些运动的形式、幅度和时间尺度的同时定量实验测定仍然难以捉摸。我们证明，使用氘代样品的相干中子散射实验可以获得这些大规模动态模式的完整描述。通过这种方法，在细胞色素 P450cam 蛋白质中建立了结构、动力学和功能之间的微观关系。这里开发的方法应该对蛋白质体系具有普遍适用性。
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