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An Efficient Labelling Approach to Harness Backbone and Side‐Chain Protons in 1 H‐Detected Solid‐State NMR Spectroscopy
Author(s) -
Mance Deni,
Sinnige Tessa,
Kaplan Mohammed,
Narasimhan Siddarth,
Daniëls Mark,
Houben Klaartje,
Baldus Marc,
Weingarth Markus
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201509170
Subject(s) - side chain , chemistry , labelling , nuclear magnetic resonance spectroscopy , spectroscopy , solid state nuclear magnetic resonance , isotopic labeling , resolution (logic) , ion , crystallography , chain (unit) , topology (electrical circuits) , stereochemistry , nuclear magnetic resonance , physics , organic chemistry , polymer , biochemistry , mathematics , quantum mechanics , artificial intelligence , combinatorics , computer science , astronomy
1 H‐detection can greatly improve spectral sensitivity in biological solid‐state NMR (ssNMR), thus allowing the study of larger and more complex proteins. However, the general requirement to perdeuterate proteins critically curtails the potential of 1 H‐detection by the loss of aliphatic side‐chain protons, which are important probes for protein structure and function. Introduced herein is a labelling scheme for 1 H‐detected ssNMR, and it gives high quality spectra for both side‐chain and backbone protons, and allows quantitative assignments and aids in probing interresidual contacts. Excellent 1 H resolution in membrane proteins is obtained, the topology and dynamics of an ion channel were studied. This labelling scheme will open new avenues for the study of challenging proteins by ssNMR.