Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Chemistry of antibody-binding to a protein

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Geysen, H. M.
  • Tainer, John
  • Rodda, S. J.
  • Mason, T. J.
  • Alexander, H.
  • Getzoff, Elizabeth
  • Lerner, Richard

publication date

  • March 1987

journal

  • Science  Journal

abstract

  • The chemistry of antibody recognition was studied by mapping the antigenicity of the protein myohemerythrin with peptide homologs of the protein sequence. The results suggest that the entire protein surface is antigenic, but the probability of there being antibodies to a given site is influenced by local stereochemistry. Although accessible to an antibody binding domain, the least reactive positions cluster in the most tightly packed and least mobile regions and are closely associated with narrow, concave grooves in the molecular surface containing bound water molecules. The most frequently recognized sites form three-dimensional superassemblies characterized by high local mobility, convex surface shape, and often by negative electrostatic potential.

subject areas

  • Antibodies
  • Antibody Formation
  • Antigens
  • Hemerythrin
  • Immunochemistry
  • Metalloproteins
  • Peptide Mapping
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.3823878

PubMed ID

  • 3823878
scroll to property group menus

Additional Document Info

start page

  • 1184

end page

  • 1190

volume

  • 235

issue

  • 4793

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support