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

Detection of a hidden folding intermediate in the focal adhesion target domain: Implications for its function and folding.

Proteins - 1 Nov 2006

Zhou Zheng, Feng Hanqiao, Bai Yawen

Abstract excerpt

The focal adhesion target (FAT) domain of focal adhesion kinase has a four-helix bundle structure. Based on a hydrogen exchange-constrained computer simulation study and some indirect experimental results, it has been suggested that a partially unfolded state of the FAT domain with the N-terminal helix unfolded plays an important role in its biological function. Here, using a native-state hydrogen exchange...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Focal Adhesion Protein-Tyrosine Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Focal Adhesions

Share to Hydrogen

Share to Protein Denaturation

Share to Protein Folding

Share to Protein Structure, Quaternary

Share to Thermodynamics

Source

Identifiers

PMID: 16909417
DOI: 10.1002/prot.21107

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

Detection of a hidden folding intermediate in the focal adhesion target domain: Implications for its function and folding.PMID 16909417Read ↗

The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin.Semantic proximity Read ↗

The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation.Semantic proximity Read ↗

Key interactions in integrin ectodomain responsible for global conformational change detected by elastic network normal-mode analysis.Semantic proximity Read ↗

The plastic energy landscape of protein folding: a triangular folding mechanism with an equilibrium intermediate for a small protein domain.Semantic proximity Read ↗

Cataract-prone variants of γD-crystallin populate a conformation with a partially unfolded N-terminal domain under native conditionsSemantic proximity Read ↗

Integrating water exclusion theory into β contacts to predict binding free energy changes and binding hot spots.Semantic proximity Read ↗

Identification of a hidden strain switch provides clues to an ancient structural mechanism in protein kinases.Semantic proximity Read ↗

Single-molecule FRET reveals hidden complexity in a protein energy landscape.Semantic proximity Read ↗

Structure and Molecular Dynamics Simulations of Protein Tyrosine Phosphatase Non-Receptor 12 Provide Insights into the Catalytic Mechanism of the Enzyme.Semantic proximity Read ↗

Mechanistic insights from replica exchange molecular dynamics simulations into mutation induced disordered-to-ordered transition in Hahellin, a βγ-crystallinSemantic proximity Read ↗

Chorography and conformational dynamism of the Soluble Human Fibrinogen in solutionSemantic proximity Read ↗

Quantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments.Semantic proximity Read ↗

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