Abstract
Two-dimensional 1H NMR spectroscopy of bovine eye lens α-crystallin and its isolated α A and α B subunits reveals that these aggregates have short and very flexible C-terminal extensions of eight (α A) and ten (α B) amino acids which adopt little preferred conformation in solution. Total α-crystallin forms a tighter aggregate than the isolated α A and α B subunit aggregates. Our results are consistent with a micelle model for α-crystallin quaternary structure. The presence of terminal extensions is a general feature of those crystallins, α and β, which form aggregates.
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