Rigidity of protein structure revealed by incoherent neutron scattering
Rigidity of protein structure revealed by incoherent neutron scattering
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非相干中子散射揭示蛋白质结构的刚性
DOI：
10.1016/j.bbagen.2020.129536
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
Kataoka Mikio
中科院分区：
文献类型：
--
作者：
Nakagawa Hiroshi;Kataoka Mikio
蛋白质的刚性和柔性反映在其结构动力学中。蛋白质动力学的研究往往集中在灵活性和柔软性，这方面的审查重点是蛋白质的结构刚性。刚性的程度可以用非相干中子散射实验评估，这是一种补充分子动力学模拟的方法。这种实验技术可以提供皮科到纳秒的时间尺度和纳米空间尺度的蛋白质动力学信息;这些动力学可以帮助通过力常数，玻色子峰，动力学转变和动力学异质性等指标量化蛋白质的刚性。这些指标还反映了蛋白质二级和三级结构的刚性。此外，这些指数还揭示了不同环境参数（如水合作用、温度、压力和蛋白质-蛋白质相互作用）对硬度的影响。水合作用对硬度和柔软度的影响比其他环境因素更大。有趣的是，水合作用以相反的方式影响谐波和非谐波运动。这种差异可能是由于蛋白质通过氢键与水分子的动态耦合。
The rigidity and flexibility of a protein is reflected in its structural dynamics. Studies on protein dynamics often focus on flexibility and softness; this review focuses on protein structural rigidity. The extent of rigidity can be assessed experimentally with incoherent neutron scattering; a method that is complementary to molecular dynamics simulation. This experimental technique can provide information about protein dynamics in timescales of pico- to nanoseconds and at spatial scales of nanometers; these dynamics can help quantify the rigidity of a protein by indices such as force constant, Boson peak, dynamical transition, and dynamical heterogeneity. These indicators also reflect the rigidity of a protein's secondary and tertiary structures. In addition, the indices reveal how rigidity is influenced by different environmental parameters, such as hydration, temperature, pressure, and protein-protein interactions. Hydration affects both rigidity and softness more than other environmental factors. Interestingly, hydration affects harmonic and anharmonic motions in opposite ways. This difference is probably due to the protein's dynamic coupling with water molecules via hydrogen bonding.