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Frontispiece: NMR Backbone Assignment of Large Proteins by Using 13 C α ‐Only Triple‐Resonance Experiments
Author(s) -
Wei Qingtao,
Chen Jiajing,
Mi Juan,
Zhang Jiahai,
Ruan Ke,
Wu Jihui
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201682862
Subject(s) - resonance (particle physics) , degenerate energy levels , covariance , nuclear magnetic resonance spectroscopy , chemistry , physics , crystallography , nuclear magnetic resonance , atomic physics , mathematics , quantum mechanics , statistics
Conformation Analysis NMR spectroscopy is a powerful method to investigate protein structure and dynamics, but backbone resonances in large proteins lead to difficulties. A covariance method utilizes the linear correlation coefficient between two degenerate 13 C α peaks to accelerate assignment; a 42 kDa MDP protein backbone was assigned with 98 % accuracy. For more details, see the Full Paper by K. Ruan, J. Wu, et al. on page 9556 ff.