TY - JOUR
T1 - Hydrogen bond strength in membrane proteins probed by time-resolved 1 H-detected solid-state NMR and MD simulations
AU - Medeiros-silva, João
AU - Jekhmane, Miranda
AU - Baldus, Marc
AU - Weingarth, Markus
PY - 2017/10/1
Y1 - 2017/10/1
N2 - 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.
AB - 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.
U2 - 10.1016/j.ssnmr.2017.03.003
DO - 10.1016/j.ssnmr.2017.03.003
M3 - Article
SN - 0926-2040
VL - 87
SP - 80
EP - 85
JO - Solid State Nuclear Magnetic Resonance
JF - Solid State Nuclear Magnetic Resonance
ER -