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疏水性探针4,4'-双(1-苯胺基-8-萘磺酸)被特异性光掺入αB-晶状体蛋白的N端结构域。

The hydrophobic probe 4,4'-bis(1-anilino-8-naphthalene sulfonic acid) is specifically photoincorporated into the N-terminal domain of alpha B-crystallin.

作者信息

Smulders R H, de Jong W W

机构信息

Department of Biochemistry, University of Nijmegen, The Netherlands.

出版信息

FEBS Lett. 1997 Jun 2;409(1):101-4. doi: 10.1016/s0014-5793(97)00498-5.

DOI:10.1016/s0014-5793(97)00498-5
PMID:9199512
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 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.

摘要

荧光探针4,4'-双（1-苯胺基-8-萘磺酸）（双-ANS）的光掺入可用于定位蛋白质中暴露于溶剂的疏水区域。我们发现双-ANS特异性地掺入αB-晶状体蛋白的假定N端结构域。这种掺入降低了αB-晶状体蛋白的伴侣样活性，表明N端结构域中的疏水表面参与了未折叠蛋白的结合。

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