期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 13, 期 1, 页码 18-24出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.1c03267
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- Max Planck Society
A new proton-detection method has been developed to measure protein torsion angles by recoupling NH and CH dipolar couplings, applicable to protonated or partly deuterated samples. The efficiency and precision of the method were demonstrated with microcrystalline chicken α-spectrin SH3 protein and the influenza A matrix 2 (M2) membrane protein. Pseudo-4D data for M2 revealed a turn between transmembrane and amphipathic helices.
Protein torsion angles define the backbone secondary structure of proteins. Magic-angle spinning (MAS) NMR methods using carbon detection have been developed to measure torsion angles by determining the relative orientation between two anisotropic interactions.dipolar coupling or chemical shift anisotropy. Here we report a new proton-detection based method to determine the backbone torsion angle by recoupling NH and CH dipolar couplings within the HCANH pulse sequence, for protonated or partly deuterated samples. We demonstrate the efficiency and precision of the method with microcrystalline chicken a spectrin SH3 protein and the influenza A matrix 2 (M2) membrane protein, using 55 or 90 kHz MAS. For M2, pseudo-4D data detect a turn between transmembrane and amphipathic helices.
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