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

Aromatic residues link binding and function of intrinsically disordered proteins.

Molecular bioSystems - 1 Jan 2012

Espinoza-Fonseca L Michel

Abstract excerpt

We have searched for intermolecular aromatic pairs in 77 protein-protein complexes of intrinsically disordered proteins (IDPs) to understand the role of π-π interactions in protein-protein interactions involving IDPs. We found that 40% of the complexes possess at least one intermolecular pair of aromatic residues. Analysis of composition, characteristics, location and the contribution to the free energy of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids, Aromatic
Share to Apoptosis Regulatory Proteins
Share to Bcl-2-Like Protein 11

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Protein Folding

Share to Protein Isoforms

Share to Protein Multimerization

Share to Thermodynamics

Source

Identifiers

PMID: 21863198
DOI: 10.1039/c1mb05239j

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Aromatic residues link binding and function of intrinsically disordered proteins.PMID 21863198Read ↗

Do intrinsically disordered proteins possess high specificity in protein-protein interactions?Semantic proximity Read ↗

How mutations of intrinsically disordered protein regions can drive cancerSemantic proximity Read ↗

Mutations of Intrinsically Disordered Protein Regions Can Drive Cancer but Lack Therapeutic Strategies.Semantic proximity Read ↗

A frustrated binding interface for intrinsically disordered proteins.Semantic proximity Read ↗

Rational drug design targeting intrinsically disordered proteinsSemantic proximity Read ↗

DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity.Semantic proximity Read ↗

Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cellSemantic proximity Read ↗

Predictive Model for Single-Site Mutations That Change Intrinsically Disordered Protein Binding Energetics.Semantic proximity Read ↗

Combined prediction and design reveals the target recognition mechanism of an intrinsically disordered protein interaction domain.Semantic proximity Read ↗

Conservation and coevolution determine evolvability of different classes of disordered residues in human intrinsically disordered proteins.Semantic proximity Read ↗

Decoding disease-causing mechanisms of missense mutations from supramolecular structures.Semantic proximity Read ↗

Protein-protein interfaces as druggable targets: A common motif of the pyridoxal-5’-phosphate-dependent enzymes to receive the coenzyme from its producersSemantic proximity Read ↗

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