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

Evaluation of disulfide bond position to enhance the thermal stability of a highly stable single domain antibody.

PloS one - 1 Jan 2014

Zabetakis Dan, Olson Mark A, Anderson George P, Legler Patricia M, Goldman Ellen R

Abstract excerpt

Single domain antibodies are the small recombinant variable domains derived from camelid heavy-chain-only antibodies. They are renowned for their stability, in large part due to their ability to refold following thermal or chemical denaturation. In addition to refolding after heat denaturation, A3, a high affinity anti-Staphylococcal Enterotoxin B single domain antibody, possesses a melting temperature of ∼84°C,...

Read the complete abstract on PubMed

Topics

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

Share to Antibody Affinity
Share to Calorimetry, Differential Scanning

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

Share to Camelids, New World

Share to Circular Dichroism

Share to Disulfides

Share to Enterotoxins

Share to Single-Domain Antibodies

Share to Transition Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 25526640
DOI: 10.1371/journal.pone.0115405
PMCID: PMC4272287

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

Evaluation of disulfide bond position to enhance the thermal stability of a highly stable single domain antibody.PMID 25526640Read ↗

Contributions of the complementarity determining regions to the thermal stability of a single-domain antibody.Semantic proximity Read ↗

Enhancing Stability of Camelid and Shark Single Domain Antibodies: An OverviewSemantic proximity Read ↗

Stabilization of an Immunoglobulin Fold Domain by an Engineered Disulfide Bond at the Buried Hydrophobic RegionSemantic proximity Read ↗

Functional Divergence in the Affinity and Stability of Non-Canonical Cysteines and Non-Canonical Disulfide Bonds: Insights from a VHH and VNAR Study.Semantic proximity Read ↗

Importance of Hypervariable Region 2 for Stability and Affinity of a Shark Single-Domain Antibody Specific for Ebola Virus NucleoproteinSemantic proximity Read ↗

Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains.Semantic proximity Read ↗

Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds.Semantic proximity Read ↗

Single antibody domains as small recognition units: design and in vitro antigen selection of camelized, human VH domains with improved protein stabilitySemantic proximity Read ↗

Improving solubility and refolding efficiency of human VHs by a novel mutational approachSemantic proximity Read ↗

Engineering an improved IgG4 molecule with reduced disulfide bond heterogeneity and increased Fab domain thermal stability.Semantic proximity Read ↗

Molecular basis for thermal stability and affinity in a VHH: Contribution of the framework region and its influence in the conformation of the CDR3Semantic proximity Read ↗

Insights into the stability of a therapeutic antibody Fab fragment by molecular dynamics and its stabilization by computational designSemantic proximity Read ↗

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