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Differences in Electrostatic Properties at Antibody–Antigen Binding Sites: Implications for Specific...

Differences in Electrostatic Properties at Antibody–Antigen Binding Sites: Implications for Specific...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1302377

Differences in Electrostatic Properties at Antibody–Antigen Binding Sites: Implications for Specificity and Cross-Reactivity

About this item

Full title

Differences in Electrostatic Properties at Antibody–Antigen Binding Sites: Implications for Specificity and Cross-Reactivity

Publisher

United States: Elsevier Inc

Journal title

Biophysical journal, 2002-12, Vol.83 (6), p.2946-2968

Language

English

Formats

Publication information

Publisher

United States: Elsevier Inc

More information

Scope and Contents

Contents

Antibodies HyHEL8, HyHEL10, and HyHEL26 (HH8, HH10, and HH26, respectively) recognize highly overlapping epitopes on hen egg-white lysozyme (HEL) with similar affinities, but with different specificities. HH8 binding to HEL is least sensitive toward mutations in the epitope and thus is most cross-reactive, HH26 is most sensitive, whereas the sensit...

Alternative Titles

Full title

Differences in Electrostatic Properties at Antibody–Antigen Binding Sites: Implications for Specificity and Cross-Reactivity

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1302377

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1302377

Other Identifiers

ISSN

0006-3495

E-ISSN

1542-0086

DOI

10.1016/S0006-3495(02)75302-2

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