A novel strategy for NMR resonance assignment and protein structure determination.
A novel strategy for NMR resonance assignment and protein structure determination.
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DOI：
10.1007/s10858-010-9458-0
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发表时间：
2011-01
影响因子：
2.7
通讯作者：
Arrowsmith CH
中科院分区：
文献类型：
--
作者：
Lemak A;Gutmanas A;Chitayat S;Karra M;Farès C;Sunnerhagen M;Arrowsmith CH
核磁共振 (NMR) 光谱测定的蛋白质结构的质量取决于实验得出的共振分配、距离和角度限制的数量和质量。蛋白质 NMR 数据的两个关键特征对中小型蛋白质的常规和自动结构测定提出了挑战； (1) 光谱分辨率——尤其是拥挤的核欧沃豪塞效应光谱 (NOESY) 光谱，以及 (2) 作为最常见分配协议的一部分，对弱标量耦合的连续网络的依赖。为了促进 NMR 结构测定，我们开发了一种半自动策略，利用非均匀采样 (NUS) 和多维分解 (MDD) 来优化数据收集和处理选定的高分辨率多维 NMR 实验，将其与用于顺序和侧链共振分配的 ABACUS 协议相结合，并简化了该程序，分别在 CYANA 和 CNS 中执行结构和细化计算。开发了两个图形用户界面（GUI）以促进数据的高效分析和编译并指导自动结构确定。这种集成方法在 30 多种大小从 5.5 kDa 到 16.5 kDa 的高质量蛋白质结构上进行了实施和完善。
The quality of protein structures determined by nuclear magnetic resonance (NMR) spectroscopy is contingent on the number and quality of experimentally-derived resonance assignments, distance and angular restraints. Two key features of protein NMR data have posed challenges for the routine and automated structure determination of small to medium sized proteins; (1) spectral resolution – especially of crowded nuclear Overhauser effect spectroscopy (NOESY) spectra, and (2) the reliance on a continuous network of weak scalar couplings as part of most common assignment protocols. In order to facilitate NMR structure determination, we developed a semi-automated strategy that utilizes non-uniform sampling (NUS) and multidimensional decomposition (MDD) for optimal data collection and processing of selected, high resolution multidimensional NMR experiments, combined it with an ABACUS protocol for sequential and side chain resonance assignments, and streamlined this procedure to execute structure and refinement calculations in CYANA and CNS, respectively. Two graphical user interfaces (GUIs) were developed to facilitate efficient analysis and compilation of the data and to guide automated structure determination. This integrated method was implemented and refined on over 30 high quality structures of proteins ranging from 5.5 to 16.5 kDa in size.
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影响因子：
2.9
作者：
Huang, YJ;Tejero, R;Montelione, GT
通讯作者：
Montelione, GT
影响因子：
2.9
作者：
IKURA, M;KAY, LE;BAX, A
通讯作者：
BAX, A
影响因子：
3.5
作者：
IKURA, M;KRINKS, M;BAX, A
通讯作者：
BAX, A
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL
影响因子：
2.7
作者：
Atreya, HS;Sahu, SC;Govil, G
通讯作者：
Govil, G