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

Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues.

Biophysical journal - 3 Jun 2009

Zhang Jinming, Lazaridis Themis

Abstract excerpt

The GxxxG sequence motif mediates the association of transmembrane (TM) helices by providing a site of close contact between them. However, it is not sufficient for strong association. For example, both bacteriophage M13 major coat protein (MCP) and human erythrocyte protein glycophorin A (GpA) contain a GxxxG motif in their TM domains and form a homodimer, but the association affinity of MCP, measured by the...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophage M13
Share to Glycophorins
Share to Membranes, Artificial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Chemical

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Multimerization

Share to Thermodynamics

Share to Viral Core Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19486666
DOI: 10.1016/j.bpj.2009.03.008
PMCID: PMC2711494

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues.PMID 19486666Read ↗

Lipid-mediated interactions tune the association of glycophorin A helix and its disruptive mutants in membranes.Semantic proximity Read ↗

Lipid solvation effects contribute to the affinity of Gly-xxx-Gly motif-mediated helix-helix interactions.Semantic proximity Read ↗

Membrane insertion and dimerization of glycophorin-A mutations studied by free energy simulations.Semantic proximity Read ↗

In silico screening of mutational effects on transmembrane helix dimerization: insights from rigid-body docking and molecular dynamics simulations.Semantic proximity Read ↗

Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer.Semantic proximity Read ↗

The association of polar residues in the DAP12 homodimer: TOXCAT and molecular dynamics simulation studies.Semantic proximity Read ↗

Motifs of serine and threonine can drive association of transmembrane helices.Semantic proximity Read ↗

Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants.Semantic proximity Read ↗

Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif.Semantic proximity Read ↗

Protein-protein association: investigation of factors influencing association rates by brownian dynamics simulations.Semantic proximity Read ↗

Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer.Semantic proximity Read ↗

Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants.Semantic proximity Read ↗

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