Inside Back Cover: Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins (Angew. Chem. Int. Ed. 2/2013)
Inside Back Cover: Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins (Angew. Chem. Int. Ed. 2/2013)
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DOI：
10.1002/anie.201209487
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发表时间：
2013-01
影响因子：
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通讯作者：
Jie-rong Huang;V. Ozenne;M. R. Jensen;M. Blackledge
中科院分区：
文献类型：
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作者：
Jie-rong Huang;V. Ozenne;M. R. Jensen;M. Blackledge
核磁共振波谱是研究无序蛋白质的强大方法，提供原子分辨率和整体平均信息。 M. Blackledge 等人在第 687 页以下的通讯中。研究表明，通过分析局部和远程效应，可以比现有技术快六个数量级来确定残余偶极耦合。
NMR spectroscopy is a powerful method for studying disordered proteins, providing atomic resolution and ensemble‐averaged information. In their Communication on page 687 ff., M. Blackledge et al. show that by analyzing local and long‐range effects, residual dipolar couplings can be determined up to six orders of magnitude faster than by existing techniques.