Residue selective 15N CEST and CPMG experiments for studies of millisecond timescale protein dynamics
- 影响因子：
0.0
- 发表刊物：
J. Magn. Reson.
- 关键字：
CEST; CPMG; Conformational exchange; Hartmann-Hahn cross-polarization transfer
- 摘要：
Proteins are intrinsically dynamic molecules and undergo exchanges among multiple conformations to perform biological functions. The CPMG relaxation dispersion and CEST experiments are two important solution NMR techniques for characterizing the conformational exchange processes on the millisecond timescale. Traditional pseudo 3D 15N CEST and CPMG experiments have certain limitations in their applications. For example, both experiments have low sensitivity for broadened resonances, and the process of optimizing sample conditions and experimental parameters are often time consuming. To overcome these limitations, we herein present a new set of residue selective 15N CEST and CPMG pulse sequences by employing the Hartmann-Hahn cross-polarization transfer of magnetization in both 1D and 2D schemes. Combined with frequency labeling in the indirect dimension using only a small number of increments, the pulse sequences in the 2D scheme can be applied on resonances in overlapped regions of the 1H-15N HSQC spectrum. The pulse sequences were further applied on several proteins, demonstrating their advantages over the traditional CEST and CPMG experiments under specific circumstances.
- 论文类型：
期刊论文
- 论文编号：
55
- 学科门类：
理学
- 卷号：
293
- 页面范围：
47-55
- 是否译文：
否
- 发表时间：
2018-08-01
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Niu Xiaogang
- 通讯作者：
Jin Changwen
- 全部作者：
Ding Jienv,Zhang Wenbo,Li Qianwen,Hu Yunfei
