Institut de Biologie Structurale, Université Grenoble Alpes , 71 Avenue des Martyrs, 38044 Grenoble Cedex 9, France.
Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), Grenoble, France.
J Am Chem Soc. 2017 Jan 25;139(3):1065-1068. doi: 10.1021/jacs.6b12089. Epub 2017 Jan 11.
NMR spectroscopy is a powerful tool for studying molecular dynamics at atomic resolution simultaneously for a large number of nuclear sites. In this communication, we combine two powerful NMR techniques, relaxation-dispersion NMR and real-time NMR, in order to obtain unprecedented information on the conformational exchange dynamics present in short-lived excited protein states, such as those transiently accumulated during protein folding. We demonstrate the feasibility of the approach for the amyloidogenic protein β2-microglobulin that folds via an intermediate state which is believed to be responsible for the onset of the aggregation process leading to amyloid formation.
NMR 光谱学是一种强大的工具，可用于同时研究大量核位点的原子分辨率的分子动力学。在本通讯中，我们结合了两种强大的 NMR 技术，弛豫分散 NMR 和实时 NMR，以获得关于短寿命激发蛋白质状态中构象交换动力学的前所未有的信息，例如在蛋白质折叠过程中短暂积累的那些状态。我们证明了该方法对于淀粉样蛋白β2-微球蛋白的可行性，该蛋白质通过中间状态折叠，该中间状态被认为是导致导致淀粉样形成的聚集过程开始的原因。
