The hydrophobic probe 4,4′‐bis(1‐anilino‐8‐naphthalene sulfonic acid) is specifically photoincorporated into the N‐terminal domain of αB‐crystallin
- 2 June 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 409 (1) , 101-104
- https://doi.org/10.1016/s0014-5793(97)00498-5
Abstract
Photoincorporation of the fluorescent probe 4,4′-bis(1-anilino-8-naphthalene sulfonic acid) (bis-ANS) can be used to locate solvent-exposed hydrophobic regions in proteins. We show that bis-ANS is specifically incorporated into the putative N-terminal domain of αB-crystallin. This incorporation diminishes the chaperone-like activity of αB-crystallin, suggesting that hydrophobic surfaces in the N-terminal domain are involved in the binding of unfolding proteins.Keywords
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