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

João Medeiros-Silva; Shehrazade Jekhmane; Marc Baldus; Markus Weingarth

doi:10.1016/j.ssnmr.2017.03.003

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

Solid State Nucl Magn Reson. 2017 Oct:87:80-85. doi: 10.1016/j.ssnmr.2017.03.003. Epub 2017 Mar 18.

Authors

João Medeiros-Silva¹, Shehrazade Jekhmane¹, Marc Baldus¹, Markus Weingarth²

Affiliations

¹ NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Department of Chemistry, Utrecht University, Pandualaan 8, 3584 CH Utrecht, The Netherlands.
² NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Department of Chemistry, Utrecht University, Pandualaan 8, 3584 CH Utrecht, The Netherlands. Electronic address: m.h.weingarth@uu.nl.

PMID: 28342732
DOI: 10.1016/j.ssnmr.2017.03.003

Abstract

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 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Hydrogen Bonding
Membrane Proteins / chemistry*
Molecular Dynamics Simulation*
Protein Conformation
Time Factors

Substances

Membrane Proteins