In:
Physical Chemistry Chemical Physics, Royal Society of Chemistry (RSC), Vol. 24, No. 35 ( 2022), p. 20803-20812
Kurzfassung:
K + channels allow selective permeation of K + , but not physiologically abundant Na + , at almost diffusion limit rates. The conduction mechanism of K + channels is still controversial, with experimental and computation studies supporting two distinct conduction mechanisms: either with or without water inside the channel. Here, we employ a bottom-up approach on hydrated alkali metal complexes of a model peptide of K + channels, Ac-Tyr-NHMe, to characterize metal–peptide, metal–water, and water–peptide interactions that govern the selectivity of K + channels at a molecular level. Both the extension to the series of alkali metal ions and to temperature-dependent studies (approaching physiological values) have revealed the clear difference between permeable and non-permeable ions in the spectral features of the ion complexes. Furthermore, the impact of hydration is discussed in relation to the K + channels by comparisons of the non-hydrated and hydrated complexes.
Materialart:
Online-Ressource
ISSN:
1463-9076
,
1463-9084
Sprache:
Englisch
Verlag:
Royal Society of Chemistry (RSC)
Publikationsdatum:
2022
ZDB Id:
1476244-4
ZDB Id:
1460656-2
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