Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
复制标题
DOI：
10.1007/s10858-008-9251-5
复制
发表时间：
2008-07-01
影响因子：
2.7
通讯作者：
Kay, Lewis E.
中科院分区：
文献类型：
--
作者：
Hansen, D. Flemming;Vallurupalli, Pramodh;Kay, Lewis E.
目前结构生物学的主要焦点是确定生物分子的静态三维表示，这些表示大部分对应于低能量（基态）构象。然而，人们越来越认识到，更高的能量结构通常在功能中也发挥着重要作用。由于这些构象异构体的含量很低，而且通常只是短暂形成，因此它们的研究不适合结构生物学的许多工具。从这个角度来看，我们讨论了基于 CPMG 的弛豫色散核磁共振波谱在表征这些低密度、不可见状态中的作用。结果表明，测量激发态主链化学位移和残余各向异性相互作用的稳健方法已经到位，并且这些数据为不可见构象异构体的结构研究提供了有价值的限制。
Currently the main focus of structural biology is the determination of static three-dimensional representations of biomolecules that for the most part correspond to low energy (ground state) conformations. However, it is becoming increasingly well recognized that higher energy structures often play important roles in function as well. Because these conformers are populated to only low levels and are often only transiently formed their study is not amenable to many of the tools of structural biology. In this perspective we discuss the role of CPMG-based relaxation dispersion NMR spectroscopy in characterizing these low populated, invisible states. It is shown that robust methods for measuring both backbone chemical shifts and residual anisotropic interactions in the excited state are in place and that these data provide valuable restraints for structural studies of invisible conformers.