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The hydrophobic probe 4,4′‐bis(1‐anilino‐8‐naphthalene sulfonic acid) is specifically photoincorporated into the N‐terminal domain of αB‐crystallin
Author(s) -
Smulders Ronald H.P.H,
de Jong Wilfried W
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00498-5
Subject(s) - naphthalene , chemistry , sulfonic acid , fluorescence , solvent , terminal (telecommunication) , stereochemistry , biophysics , biochemistry , organic chemistry , biology , physics , quantum mechanics , telecommunications , computer science
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.