Conserved aromatic residues as determinants in the folding and assembly of immunoglobulin variable domains
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文摘

Immunoglobulin VH and VL domains exhibit both shared and unique sites of conservation.

Ig heavy- and light-chains share critical sites of conserved aromaticity.

Conserved aromaticity is symmetrically concentrated in the VH–VL interface.

A role for aromaticity in both the folding and assembly of antibody structure is postulated.

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