Dual Conformations of an Immunoglobulin Light-Chain Dimer. Heterogeneity of Antigen Specificity and Idiotope Profile May Result from Multiple Variable-Domain Interaction Mechanisms

The structure of an immunoglobulin antigenbinding fragment (Fab) has been thought to be invariantly defined by well-conserved amino acid residues in the variable domains of the heavy and light chains. These conserved residues enable folding of the polypeptide segments into the characteristic immunog...

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