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

Exploring the conformational transition between the fully folded and locally unfolded substates of Escherichia coli thiol peroxidase.

Physical chemistry chemical physics : PCCP - 7 May 2020

Vazquez Diego S, Zeida Ari, Agudelo William A, Montes Mónica R, Ferrer-Sueta Gerardo, Santos Javier

Abstract excerpt

Thiol peroxidase from Escherichia coli (EcTPx) is a peroxiredoxin that catalyzes the reduction of different hydroperoxides. During the catalytic cycle of EcTPx, the peroxidatic cysteine (CP) is oxidized to a sulfenic acid by peroxide, then the resolving cysteine (CR) condenses with the sulfenic acid of CP to form a disulfide bond, which is finally reduced by thioredoxin. Purified EcTPx as dithiol and disulfide...

Read the complete abstract on PubMed

Topics

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

Share to Computer Simulation
Share to Escherichia coli

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

Share to Escherichia coli Proteins

Share to Molecular Dynamics Simulation

Share to Periplasmic Proteins

Share to Peroxidases

Share to Protein Conformation

Share to Protein Folding

Source

Identifiers

PMID: 32319475
DOI: 10.1039/d0cp00140f

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploring the conformational transition between the fully folded and locally unfolded substates of Escherichia coli thiol peroxidase.PMID 32319475Read ↗

Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins.Semantic proximity Read ↗

Systematic conformation-to-phenotype mapping via limited deep-sequencing of proteinsSemantic proximity Read ↗

Structural characteristics of the redox-sensing coiled coil in the voltage-gated H+ channel.Semantic proximity Read ↗

Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase.Semantic proximity Read ↗

Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants.Semantic proximity Read ↗

Compact conformations of human protein disulfide isomerase.Semantic proximity Read ↗

Key roles of the Escherichia coli AhpC C-terminus in assembly and catalysis of alkylhydroperoxide reductase, an enzyme essential for the alleviation of oxidative stress.Semantic proximity Read ↗

Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis.Semantic proximity Read ↗

Investigating the Molecular Mechanisms Behind Uncharacterized Cysteine Losses from Prediction of Their Oxidation State.Semantic proximity Read ↗

Structural features of human DJ-1 in distinct Cys106 oxidative states and their relevance to its loss of function in disease.Semantic proximity Read ↗

Role of the disulfide bond in stabilizing and folding of the fimbrial protein DraE from uropathogenic Escherichia coli.Semantic proximity Read ↗

Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2.Semantic proximity Read ↗

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