The hydrophobic probe 4,4′‐bis(1‐anilino‐8‐naphthalene sulfonic acid) is specifically photoincorporated into the N‐terminal domain of αB‐crystallin

FEBS Letters

de Jong, Wilfried W¹  Smulders, Ronald H.P.H¹ 

[1] Department of Biochemistry, University of Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands

关键词: αB-Crystallin;    Small heat shock protein;    Chaperone-like activity;    Photolabeling;    bis-ANS;    4;    4′-bis(1-anilino-8-naphthalene sulfonic acid);    hsp;    heat shock protein(s);   

DOI  :  10.1016/S0014-5793(97)00498-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown