Identification by 1H NMR spectroscopy of flexible C‐terminal extensions in bovine lens α‐crystallin
- 19 October 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 311 (2), 143-149
- https://doi.org/10.1016/0014-5793(92)81386-z
Abstract
Two‐dimensional 1H NMR spectroscopy of bovine eye lens α‐crystallin and its isolated αA and αB subunits reveals that these aggregates have short and very flexible C‐terminal extensions of eight (αA) and ten (αB) amino acids which adopt little preferred conformation in solution. Total α‐crystallin forms a tighter aggregate than the isolated αA and αB 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.Keywords
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