Protein crystallography is frequently used to obtain the atomic‐resolution structure of a particular protein by x‐ray diffraction of its crystallized form. Nevertheless, a single static structure cannot represent the sequence structural dynamics of a protein's function. Based on our previous study (J. Phys. Chem. B 2017, 121 (50), 11229–11240 and ACS Catal. 2018, 8 (3), 2534–2545), we herein introduce a strategy of determining the protein hydration structures by small‐angle X‐ray and neutron scattering (SAXS and SANS) with contrast variation techniques, in combination with molecular dynamics simulation (MD), to describe hydrodynamics conformation transitions of biomacromolecules. Water is a partner that conducts the dynamics of proteins, and hydration interactions with proteins affect their dynamics. To shed light on the way of the chemical constitution of a protein, the water interactions, and the dynamics of its structure underlie the specific mechanisms of enzyme functions, we review an integrated approach using small‐angle X‐ray and neutron scattering (SAXS and SANS) in combination with molecular dynamics (MD) simulation to probe the structural dynamics of a given protein, thus shedding light on its function.

中文翻译：

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分子动力学模拟结合小角度X射线/中子散射定义溶液状态蛋白质结构

蛋白质晶体学常用于通过结晶形式的X射线衍射来获得特定蛋白质的原子分辨结构。然而，单个静态结构不能代表蛋白质功能的序列结构动力学。根据我们以前的研究（J.物理学。化学式乙2017年，121（50），11229-11240和ACS CATAL。2018，8（3），2534–2545年），我们在此介绍一种通过对比分析技术结合分子动力学模拟（MD）通过小角度X射线和中子散射（SAXS和SANS）确定蛋白质水合结构的策略，描述生物大分子的流体动力学构象转变。水是传导蛋白质动力学的伙伴，与蛋白质的水合相互作用会影响其动力学。为了阐明蛋白质的化学组成方式，水相互作用以及其结构的动力学是酶功能的特定机制的基础，我们回顾了使用小角度X射线和中子散射（SAXS和SANS）与分子动力学（MD）模拟相结合，以探测给定蛋白质的结构动力学，