Protein internal dynamics is essential for its function. Exploring the internal dynamics of protein molecules as well as its connection to protein structure and function is a central topic in biophysics. However, the atomic motions in protein molecules exhibit a great degree of complexities. These complexities arise from the complex chemical composition and superposition of different types of atomic motions on the similar time scales, and render it challenging to explicitly understand the microscopic mechanism governing protein motions, functions, and their connections. Here, we demonstrate that, by using neutron scattering, molecular dynamics simulation, and deuteration technique, one can address this challenge to a large extent.

蛋白质内部动力学对其功能至关重要。探索蛋白质分子的内部动力学及其与蛋白质结构和功能的联系是生物物理学的中心课题。但是，蛋白质分子中的原子运动表现出高度的复杂性。这些复杂性源于复杂的化学组成以及在相似的时间尺度上不同类型的原子运动的叠加，因此要明确了解支配蛋白质运动，功能及其联系的微观机制将面临挑战。在这里，我们证明，通过使用中子散射，分子动力学模拟和氘化技术，人们可以在很大程度上解决这一挑战。