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 influence of disulfide bonds on the mechanical stability of proteins is context dependent.

The Journal of biological chemistry - 11 Aug 2017

Manteca Aitor, Alonso-Caballero Álvaro, Fertin Marie, Poly Simon, De Sancho David, Perez-Jimenez Raul

Abstract excerpt

Disulfide bonds play a crucial role in proteins, modulating their stability and constraining their conformational dynamics. A particularly important case is that of proteins that need to withstand forces arising from their normal biological function and that are often disulfide bonded. However, the influence of disulfides on the overall mechanical stability of proteins is poorly understood. Here, we used...

Read the complete abstract on PubMed

Topics

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

Share to Connectin
Share to Cystine
Share to Fimbriae Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Engineering

Share to Protein Interaction Domains and Motifs

Share to Protein Stability

Share to Protein Unfolding

Share to Single Molecule Imaging

Source

Open in PubMed Open full text

Identifiers

PMID: 28642368
DOI: 10.1074/jbc.M117.784934
PMCID: PMC5555196

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

The influence of disulfide bonds on the mechanical stability of proteins is context dependent.PMID 28642368Read ↗

Tailoring protein nanomechanics with chemical reactivity.Semantic proximity Read ↗

Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy.Semantic proximity Read ↗

Hidden complexity in the mechanical properties of titin.Semantic proximity Read ↗

Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes.Semantic proximity Read ↗

Engineered bi-histidine metal chelation sites map the structure of the mechanical unfolding transition state of an elastomeric protein domain GB1.Semantic proximity Read ↗

Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding versus global unfolding.Semantic proximity Read ↗

Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains.Semantic proximity Read ↗

The Y9P Variant of the Titin I27 Module: Structural Determinants of Its Revisited Nanomechanics.Semantic proximity Read ↗

Dynamic Disulfide Bond Topologies in von-Willebrand-Factor’s C4-Domain Undermine Platelet BindingSemantic proximity Read ↗

Point mutations alter the mechanical stability of immunoglobulin modules.Semantic proximity Read ↗

Basal oxidation of conserved cysteines modulates cardiac titin stiffness and dynamicsSemantic proximity Read ↗

β-sheet-like formation during the mechanical unfolding of prion protein.Semantic proximity Read ↗

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