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): João 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 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.
Graphical abstract

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