Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Anion pathway and potential energy profiles along curvilinear bacterial ClC Cl- pores: electrostatic effects of charged residues.

Biophysical journal - 1 Feb 2004

Miloshevsky Gennady V, Jordan Peter C

Abstract excerpt

X-ray structures permit theoretical study of Cl(-) permeation along bacterial ClC Cl(-) pores. We determined the lowest energy curvilinear pathway, identified anion-coordinating amino acids, and calculated the electrostatic potential energy profiles. We find that all four bacterial ClC Cl(-) crystal structures correspond to closed states. E148 and S107 side chains form steric barriers on both sides of the crystal...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anions
Share to Chloride Channels
Share to Chlorine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Energy Transfer

Share to Ion Channel Gating

Share to Models, Chemical

Share to Porosity

Share to Static Electricity

Source

Open in PubMed Open full text

Identifiers

PMID: 14747318
DOI: 10.1016/S0006-3495(04)74158-2
PMCID: PMC1303930

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Anion pathway and potential energy profiles along curvilinear bacterial ClC Cl- pores: electrostatic effects of charged residues.PMID 14747318Read ↗

Influences of mutations on the electrostatic binding free energies of chloride ions in Escherichia coli ClC.Semantic proximity Read ↗

Mutations in an intracellular vestibule that bifurcates from the pore of ClC-1 chloride ion channels affect anion permeationSemantic proximity Read ↗

Divergent Cl <sup>−</sup> and H <sup>+</sup> pathways underlie transport coupling and gating in CLC exchangers and channelsSemantic proximity Read ↗

Separate ion pathways in a Cl-/H+ exchanger.Semantic proximity Read ↗

Ion transit pathways and gating in ClC chloride channels.Semantic proximity Read ↗

Intracellular proton access in a Cl(-)/H(+) antiporter.Semantic proximity Read ↗

Structure and function of ClC chloride channels.Semantic proximity Read ↗

Ion-binding properties of the ClC chloride selectivity filter.Semantic proximity Read ↗

Structure of a slow CLC Cl⁻/H+ antiporter from a cyanobacterium.Semantic proximity Read ↗

Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.Semantic proximity Read ↗

A CLC-ec1 mutant reveals global conformational change and suggests a unifying mechanism for the CLC Cl-/H+ transport cycle.Semantic proximity Read ↗

Proton sensing of CLC-0 mutant E166D.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.