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

How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme?

Protein science : a publication of the Protein Society - 1 Oct 2002

Pons Jaume, Stratton Jennifer R, Kirsch Jack F

Abstract excerpt

The anti-hen egg-white lysozyme (HEWL) antibodies HyHEL-10 and F9.13.7 recognize a common epitope. The structures of the complexes differ, however, in the numbers of electrostatic and hydrogen-bond interactions and in the distributions of contacts between the light and heavy chains. The equilibria and kinetics characterizing the F9.13.7 complex formation were evaluated for both wild-type and mutant derivatives of...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies
Share to Antibody Affinity
Share to Antibody Specificity

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

Share to Conserved Sequence

Share to Egg Proteins

Share to Epitope Mapping

Share to Epitopes

Share to Muramidase

Source

Open in PubMed Open full text

Identifiers

PMID: 12237453
DOI: 10.1110/ps.0209102
PMCID: PMC2373715

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

How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme?PMID 12237453Read ↗

Association energetics of cross-reactive and specific antibodies.Semantic proximity Read ↗

Structural consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10.Semantic proximity Read ↗

Thermodynamics of antibody-antigen interaction revealed by mutation analysis of antibody variable regions.Semantic proximity Read ↗

Crystal structure of a cross-reaction complex between Fab F9.13.7 and guinea fowl lysozyme.Semantic proximity Read ↗

Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL.Semantic proximity Read ↗

Structural differences among monoclonal antibodies with distinct fine specificities and kinetic properties.Semantic proximity Read ↗

Mutation of Framework Residue H71 Results in Different Antibody Paratope States in Solution.Semantic proximity Read ↗

Immunological optimization of a generic hydrophobic pocket for high affinity hapten binding and Diels-Alder activity.Semantic proximity Read ↗

Analysis of protein-protein interactions and the effects of amino acid mutations on their energetics. The importance of water molecules in the binding epitope.Semantic proximity Read ↗

Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes.Semantic proximity Read ↗

Crystal structure of an Fv-Fv idiotope-anti-idiotope complex at 1.9 A resolution.Semantic proximity Read ↗

Thermodynamic consequences of grafting enhanced affinity toward the mutated antigen onto an antibody. The case of anti-lysozyme antibody, HyHEL-10.Semantic proximity Read ↗

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