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 folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.

Nature structural biology - 1 Nov 1999

Martínez J C, Serrano L

Abstract excerpt

The protein engineering analysis of the alpha-spectrin SH3 domain at three different stability conditions (pH 7.0, 3.5 and 2.5) reveals a folding transition state structured around the distal loop beta-hairpin and the 310-helix. This region is impervious to overall changes in protein stability, s...

Read the complete abstract on PubMed

Topics

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

Share to Conserved Sequence
Share to Hydrogen-Ion Concentration
Share to Protein Denaturation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Spectrin

Share to src Homology Domains

Share to Thermodynamics

Source

Identifiers

PMID: 10542091
DOI: 10.1038/14896

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-10542091-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.PMID 10542091Read ↗

Conformational strain in the hydrophobic core and its implications for protein folding and design.Semantic proximity Read ↗

Role of native topology investigated by multiple unfolding simulations of four SH3 domains.Semantic proximity Read ↗

Atomic resolution structure of a mutant of the spectrin SH3 domain.Semantic proximity Read ↗

The SH3-fold family: experimental evidence and prediction of variations in the folding pathways.Semantic proximity Read ↗

Similarities between the spectrin SH3 domain denatured state and its folding transition state.Semantic proximity Read ↗

Different folding transition states may result in the same native structure.Semantic proximity Read ↗

Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium.Semantic proximity Read ↗

Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils.Semantic proximity Read ↗

High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.Semantic proximity Read ↗

Stiffness of the distal loop restricts the structural heterogeneity of the transition state ensemble in SH3 domains.Semantic proximity Read ↗

Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.Semantic proximity Read ↗

A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation.Semantic proximity Read ↗

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