Hydration Mimicry by Membrane Ion Channels

Annual Review of Physical Chemistry
M I ChaudhariS B Rempe

Abstract

Ions transiting biomembranes might pass readily from water through ion-specific membrane proteins if these protein channels provide environments similar to the aqueous solution hydration environment. Indeed, bulk aqueous solution is an important reference condition for the ion permeation process. Assessment of this hydration mimicry concept depends on understanding the hydration structure and free energies of metal ions in water in order to provide a comparison for the membrane channel environment. To refine these considerations, we review local hydration structures of ions in bulk water and the molecular quasi-chemical theory that provides hydration free energies. In doing so, we note some current views of ion binding to membrane channels and suggest new physical chemical calculations and experiments that might further clarify the hydration mimicry concept. Expected final online publication date for the Annual Review of Physical Chemistry, Volume 71 is April 20, 2020. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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Citations

Feb 4, 2021·The Journal of Physical Chemistry. B·Man Thi Hong NguyenPavel Jungwirth
Nov 19, 2020·Proceedings of the National Academy of Sciences of the United States of America·Yu Shi, Thomas L Beck
Feb 24, 2021·The Journal of Physical Chemistry. B·Andrew E Eisenhart, Thomas L Beck
Jun 3, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Diego T GomezSusan B Rempe
Jul 15, 2021·Chemical Science·Zhifeng JingPengyu Ren

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Methods Mentioned

BETA
X-ray
neutron scattering
dissection

Software Mentioned

QCT
AIMD

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