The hydrophobic probe 4,4'-bis(1-anilino-8-naphthalene sulfonic acid) is specifically photoincorporated into the N-terminal domain of alpha B-crystallin.
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 alpha B-crystallin. This incorporation diminishes the chaperone-like activity of alpha B-crystallin, suggesting that hydrophobic surfaces in the N-terminal domain are involved in the binding of unfolding proteins.
Smulders
R H
RH
Department of Biochemistry, University of Nijmegen, The Netherlands.
de Jong
W W
WW
D000595:Amino Acid Sequence; D000817:Anilino Naphthalenesulfonates / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D003459:Crystallins / Q000737:chemistry / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000737:chemistry / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism; D010777:Photochemistry; D017434:Protein Structure, Tertiary; D051381:Rats; D013379:Substrate Specificity
D000817:Anilino Naphthalenesulfonates; D003459:Crystallins; D005456:Fluorescent Dyes; D006360:Heat-Shock Proteins; C035763:5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)