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New Views of Multi-Ion Channels

Lester, Henry A. and Dougherty, Dennis A. (1998) New Views of Multi-Ion Channels. Journal of General Physiology, 111 (2). pp. 181-183. ISSN 0022-1295. PMCID PMC2222761. http://resolver.caltech.edu/CaltechAUTHORS:LESjgp98

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Abstract

Thus, most site-directed mutagenesis data render it untenable to consider that two or more roughly equivalent high affinity sites govern selectivity in multi-ion pores. The papers by Dang and McCleskey and Kiss et al. respond to this challenge by showing that a model with a single high affinity site, flanked by two binding sites of lower affinity close to the pore entrances, can generate much of the classical multi-ion behavior. The sites need not interact, and the two flanking sites could arise from one of several mechanisms: a featureless charged vestibule, a dehydration step, or a specific weak binding site. The multi-ion pore remains a cornerstone of permeation theory, but the new theory features only a single high affinity site and no mutual repulsion. The high flux rate occurs because ions pause at the flanking sites and reequilibrate thermally, gaining enough energy to move over the next barrier.


Item Type:Article
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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2222761/PubMed CentralArticle
ORCID:
AuthorORCID
Lester, Henry A.0000-0002-5470-5255
Dougherty, Dennis A.0000-0003-1464-2461
Additional Information:© 1998 by The Rockefeller University Press. fter the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof. Commentary.
PubMed Central ID:PMC2222761
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Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:LESjgp98
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ID Code:6585
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Deposited On:13 Dec 2006
Last Modified:07 Nov 2017 23:53

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