Institut des Sciences et Ingénierie Chimiques , Ecole Polytechnique Fédérale de Lausanne (EPFL) , 1015 Lausanne , Switzerland.
Université Grenoble Alpes, CNRS, CEA, IBS , 38000 Grenoble , France.
J Phys Chem B. 2018 Oct 25;122(42):9697-9702. doi: 10.1021/acs.jpcb.8b08578. Epub 2018 Oct 10.
Understanding the interplay between protein function and dynamics is currently one of the fundamental challenges of physical biology. Recently, a method using variable temperature solid-state nuclear magnetic resonance relaxation measurements has been proposed for the simultaneous measurement of 12 different activation energies reporting on distinct dynamic modes in the protein GB1. Here, we extend this approach to measure relaxation at multiple magnetic field strengths, allowing us to better constrain the motional models and to simultaneously evaluate the robustness and physical basis of the method. The data reveal backbone and side-chain motions, exhibiting low- and high-energy modes with temperature coefficients around 5 and 25 kJ·mol. The results are compared to variable temperature molecular dynamics simulation of the crystal lattice, providing further support for the interpretation of the experimental data in terms of molecular motion.
理解蛋白质功能和动力学之间的相互作用是物理生物学目前面临的基本挑战之一。最近，提出了一种使用变温固态核磁共振弛豫测量的方法，用于同时测量蛋白质 GB1 中 12 种不同的激活能，以报告不同的动态模式。在这里，我们扩展了这种方法来测量多个磁场强度下的弛豫，这使我们能够更好地约束运动模型，并同时评估该方法的稳健性和物理基础。实验数据揭示了骨架和侧链运动，表现出具有 5 和 25 kJ·mol 左右温度系数的低能和高能模式。结果与晶体点阵的变温分子动力学模拟进行了比较，为根据分子运动对实验数据的解释提供了进一步的支持。
