Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.
Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.
复制标题
蛋白质动力学研究中距离无关的互相关弛豫和各向同性化学位移调制。
DOI：
10.1002/cphc.201800602
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发表时间：
2019
期刊：
影响因子：
--
通讯作者：
Vugmeyster,Liliya
中科院分区：
文献类型：
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作者：
Vögeli,Beat;Vugmeyster,Liliya
多量子相干态中的交叉相关弛豫（CCR）与其他弛豫现象不同，因为它的理论能力是在无限远的距离上进行调解。这两种干扰弛豫机制可以是偶极相互作用、化学位移各向异性、化学位移调制或四极相互作用。这些特性使得多量子CCR成为其他测量无法获得的生物大分子结构和动力学的有吸引力的探针。在这里，我们回顾了多量子CCR测量在蛋白质动力学研究中的应用。我们编制了一份清单，建议CCR率测量的所有实验，提供了一个概述的理论，重点是蛋白质动力学，并提出了各种蛋白质系统的应用。
Cross‐correlated relaxation (CCR) in multiple‐quantum coherences differs from other relaxation phenomena in its theoretical ability to be mediated across an infinite distance. The two interfering relaxation mechanisms may be dipolar interactions, chemical shift anisotropies, chemical shift modulations or quadrupolar interactions. These properties make multiple‐quantum CCR an attractive probe for structure and dynamics of biomacromolecules not accessible from other measurements. Here, we review the use of multiple‐quantum CCR measurements in dynamics studies of proteins. We compile a list of all experiments proposed for CCR rate measurements, provide an overview of the theory with a focus on protein dynamics, and present applications to various protein systems.