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

The cost of living in the membrane: a case study of hydrophobic mismatch for the multi-segment protein LeuT.

Chemistry and physics of lipids - 1 Apr 2013

Mondal Sayan, Khelashvili George, Shi Lei, Weinstein Harel

Abstract excerpt

Many observations of the role of the membrane in the function and organization of transmembrane (TM) proteins have been explained in terms of hydrophobic mismatch between the membrane and the inserted protein. For a quantitative investigation of this mechanism in the lipid-protein interactions of functionally relevant conformations adopted by a multi-TM segment protein, the bacterial leucine transporter (LeuT),...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Phosphatidylethanolamines

Share to Phosphatidylglycerols

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 23376428
DOI: 10.1016/j.chemphyslip.2013.01.006
PMCID: PMC3631462

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The cost of living in the membrane: a case study of hydrophobic mismatch for the multi-segment protein LeuT.PMID 23376428Read ↗

Properties of an inward-facing state of LeuT: conformational stability and substrate release.Semantic proximity Read ↗

Spontaneous Inward Opening of the Dopamine Transporter Is Triggered by PIP2-Regulated Dynamics of the N-TerminusSemantic proximity Read ↗

Mechanism of the Association between Na+ Binding and Conformations at the Intracellular Gate in Neurotransmitter:Sodium Symporters.Semantic proximity Read ↗

Double-Transmembrane Domain of SNAREs Decelerates the Fusion by Increasing the Protein-Lipid Mismatch.Semantic proximity Read ↗

Molecular mechanism of substrate specificity in the bacterial neutral amino acid transporter LeuT.Semantic proximity Read ↗

Microseconds simulations reveal a new sodium-binding site and the mechanism of sodium-coupled substrate uptake by LeuT.Semantic proximity Read ↗

Substrate-modulated gating dynamics in a Na+-coupled neurotransmitter transporter homologue.Semantic proximity Read ↗

How structural elements added by evolution from bacterial transporters to human SLC6 homologs have enabled new functional propertiesSemantic proximity Read ↗

Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT.Semantic proximity Read ↗

The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect.Semantic proximity Read ↗

Local Bilayer Hydrophobicity Modulates Membrane Protein StabilitySemantic proximity Read ↗

Exploring the nature of the translocon-assisted protein insertion.Semantic proximity Read ↗

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