Thread: Hydrogen bond strength in membrane proteins by time-resolved 1H-detected solid-state NMR and MD simulations
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Default 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

Author(s): Joćo Medeiros-Silva, Shehrazade Jekhmane, Marc Baldus, Markus Weingarth

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 hydrogen bonds by combining time-resolved 1H-detected solid-state NMR 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.
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