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  • Title: Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin.
    Author: Carver JA, Aquilina JA, Truscott RJ, Ralston GB.
    Journal: FEBS Lett; 1992 Oct 19; 311(2):143-9. PubMed ID: 1397302.
    Abstract:
    Two-dimensional 1H NMR spectroscopy of bovine eye lens alpha-crystallin and its isolated alpha A and alpha B subunits reveals that these aggregates have short and very flexible C-terminal extensions of eight (alpha A) and ten (alpha B) amino acids which adopt little preferred conformation in solution. Total alpha-crystallin forms a tighter aggregate than the isolated alpha A and alpha B subunit aggregates. Our results are consistent with a micelle model for alpha-crystallin quaternary structure. The presence of terminal extensions is a general feature of those crystallins, alpha and beta, which form aggregates.
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