Mapping an Equilibrium Folding Intermediate of the Cytolytic Pore Toxin ClyA with Single-Molecule FRET.

doi:10.1021/acs.jpcb.8b07026

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

Community

Back to search

Article

Mapping an Equilibrium Folding Intermediate of the Cytolytic Pore Toxin ClyA with Single-Molecule FRET.

The journal of physical chemistry. B - 13 Dec 2018

Dingfelder Fabian, Benke Stephan, Nettels Daniel, Schuler Benjamin

Abstract excerpt

The 303-residue cytolytic toxin ClyA forms a stable α-helical monomer. In the presence of detergents or membranes, however, the protein makes a large conformational transition to the protomer state, which is competent for assembly into a dodecameric cytolytic pore. In this study, we map the structure of the ClyA monomer during denaturant-induced unfolding with single-molecule Förster resonance energy transfer...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli
Share to Escherichia coli Proteins
Share to Fluorescence Resonance Energy Transfer

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Guanidine

Share to Hemolysin Proteins

Share to Mutagenesis, Site-Directed

Share to Protein Conformation, alpha-Helical

Share to Protein Denaturation

Source

Open in PubMed

Identifiers

PMID: 30156409
DOI: 10.1021/acs.jpcb.8b07026

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.