An Efficient Labelling Approach to Harness Backbone and Side‐Chain Protons in 1H‐Detected Solid‐State NMR Spectroscopy. Issue 52 (11th November 2015)

• Record Type: Journal Article
• Authors: Mance, Deni; Sinnige, Tessa; Kaplan, Mohammed; Narasimhan, Siddarth; Daniëls, Mark; Houben, Klaartje; Baldus, Marc; Weingarth, Markus
• Is Part Of: Angewandte Chemie international edition. Volume 54:Issue 52(2015)
• Page Start: 15799
• Page End: 15803
• Publication Date: 2015-11-11
• Subjects: ion channels -- membrane proteins -- proton detection -- side‐chain protons -- solid‐state NMR spectroscopy; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201509170
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: 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. Abstract : Solid gains : Fractional deuteration in 1 H‐detected solid‐state NMR provides powerful access to exchangeable and non‐exchangeable protons without losing much, if any, spectral resolution compared to that of proteins which are devoid of non‐exchangeable protons. Fractional deuteration was successfully applied to study membrane topology and supramolecular interactions of an ion channel.