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Article

Association energetics of cross-reactive and specific antibodies.

Biochemistry - 17 Feb 2009

Mohan S, Kourentzi Katerina, Schick Kari A, Uehara Christian, Lipschultz Claudia A, Acchione Mauro, Desantis Morgan E, Smith-Gill Sandra J, Willson Richard C

Abstract excerpt

HyHEL-8, HyHEL-10, and HyHEL-26 (HH8, HH10, and HH26, respectively) are murine monoclonal IgG(1) antibodies which share over 90% variable-region amino acid sequence identity and recognize identical structurally characterized epitopes on hen egg white lysozyme (HEL). Previous immunochemical and surface plasmon resonance-based studies have shown that these antibodies differ widely in their tolerance of mutations in...

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Identifiers

PMID: 19166328
DOI: 10.1021/bi801901d
PMCID: PMC2713044

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Association energetics of cross-reactive and specific antibodies.PMID 19166328Read ↗

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Structural basis of antibody-antigen interactions.Semantic proximity Read ↗

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

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

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

Observation of redistribution for local conformational dynamics in cross-reactive antibody design.Semantic proximity Read ↗

Exploring the energy landscape of antibody-antigen complexes: protein dynamics, flexibility, and molecular recognition.Semantic proximity Read ↗

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

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