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Default (1) H-Detected Solid-State NMR Studies of Water-Inaccessible Proteins In Vitro and In Situ.

(1) H-Detected Solid-State NMR Studies of Water-Inaccessible Proteins In Vitro and In Situ.

Related Articles (1) H-Detected Solid-State NMR Studies of Water-Inaccessible Proteins In Vitro and In Situ.

Angew Chem Int Ed Engl. 2016 Sep 27;

Authors: Medeiros-Silva J, Mance D, DaniŽls M, Jekhmane S, Houben K, Baldus M, Weingarth M

Abstract
(1) H detection can significantly improve solid-state NMR spectral sensitivity and thereby allows studying more complex proteins. However, the common prerequisite for (1) H detection is the introduction of exchangeable protons in otherwise deuterated proteins, which has thus far significantly hampered studies of partly water-inaccessible proteins, such as membrane proteins. Herein, we present an approach that enables high-resolution (1) H-detected solid-state NMR (ssNMR) studies of water-inaccessible proteins, and that even works in highly complex environments such as cellular surfaces. In particular, the method was applied to study the K(+) channel KcsA in liposomes and in situ in native bacterial cell membranes. We used our data for a dynamic analysis, and we show that the selectivity filter, which is responsible for ion conduction and highly conserved in K(+) channels, undergoes pronounced molecular motion. We expect this approach to open new avenues for biomolecular ssNMR.


PMID: 27671832 [PubMed - as supplied by publisher]



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