Related ArticlesHydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations.
Solid State Nucl Magn Reson. 2017 Mar 18;:
Authors: Medeiros-Silva J, Jekhmane S, Baldus M, Weingarth M
Abstract
(1)H-detected solid-state NMR in combination with (1)H/(2)D exchange steps allows for the direct identification of very strong hydrogen bonds in membrane proteins. On the example of the membrane-embedded potassium channel KcsA, we quantify the longevity of such very strong hydrogen bonds by combining time-resolved (1)H-detected solid-state NMR experiments and molecular dynamics simulations. In particular, we show that the carboxyl-side chain of the highly conserved residue Glu51 is involved in ultra-strong hydrogen bonds, which are fully-water-exposed and yet stable for weeks. The astonishing stability of these hydrogen bonds is important for the structural integrity of potassium channels, which we further corroborate by computational studies.
PMID: 28342732 [PubMed - as supplied by publisher]
Hydrogen bond strength in membrane proteins by time-resolved 1H-detected solid-state NMR and MD simulations
Hydrogen bond strength in membrane proteins by time-resolved 1H-detected solid-state NMR and MD simulations
Publication date: Available online 18 March 2017
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Joćo Medeiros-Silva, Shehrazade Jekhmane, Marc Baldus, Markus Weingarth</br>
1H-detected solid-state NMR in combination with 1H/2D exchange steps allows for the direct identification of very strong hydrogen bonds in membrane proteins. On the example of the membrane-embedded potassium channel KcsA, we quantify the longevity of such very strong...
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Hydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations.
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