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

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

The Journal of biological chemistry - 28 Apr 2000

Nishimiya Y, Tsumoto K, Shiroishi M, Yutani K, Kumagai I

Abstract excerpt

In order to address the mechanism of enhancement of the affinity of an antibody toward an antigen from a thermodynamic viewpoint, anti-hen lysozyme (HEL) antibody HyHEL-10, which also recognize the mutated antigen turkey lysozyme (TEL) with reduced affinity, was examined. Grafting high affinity t...

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 Antibody Specificity
Share to Calorimetry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Entropy

Share to Immunoglobulin Fragments

Share to Muramidase

Share to Peptide Library

Share to Turkeys

Source

Identifiers

PMID: 10777579
DOI: 10.1074/jbc.275.17.12813

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-10777579-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Thermodynamic consequences of grafting enhanced affinity toward the mutated antigen onto an antibody. The case of anti-lysozyme antibody, HyHEL-10.PMID 10777579Read ↗

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

Critical contribution of VH–VL interaction to reshaping of an antibody: The case of humanization of anti‐lysozyme antibody, HyHEL‐10Semantic 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 consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10.Semantic proximity Read ↗

Thermodynamic Consequences of Mutations in Vernier Zone Residues of a Humanized Anti-human Epidermal Growth Factor Receptor Murine Antibody, 528Semantic proximity Read ↗

Light chain somatic mutations change thermodynamics of binding and water coordination in the HyHEL-10 family of antibodies.Semantic proximity Read ↗

Strategy for affinity maturation of an antibody with high evolvability to (4-hydroxy-3-nitrophenyl) acetyl hapten.Semantic proximity Read ↗

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

Experimental analysis by site-directed mutagenesis of somatic mutation effects on affinity and fine specificity in antibodies specific for lysozyme.Semantic proximity Read ↗

Increasing the melting temperature of VHH with the in silico free energy score.Semantic proximity Read ↗

Affinity Maturation for Antibody Engineering: The Critical Role of Residues on CDR Loops of Antibodies in Antigen BindingSemantic proximity Read ↗

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

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