The accessibility of peptides bound to the mouse MHC class II molecule IEd studied by fluorescence

FEBS Letters

de Kroon, Anton I.P.M.¹ 

[1] Department of Chemistry, Stanford University, Stanford, CA 94305, USA

关键词: MHC class II;    Fluorescence quenching;    Fluorescein-labeled peptide;    NBD-labeled peptide;    MHC;    major histocompatibility complex;    HEL;    hen egg lysozyme 107-116;    dyn;    dynorphin A 1–13;    TEMPOL;    4-hydroxy-2;    2;    6;    6-tetramethylpiperidinyloxy;    F;    fluorescein;    NBD;    7-nitro-benz-2-oxa-1;    3-diazole;    ACP;    acyl carrier protein 65–74;   

DOI  :  10.1016/0014-5793(94)80507-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The accessibility of fluorescently labeled (antigenic) peptides bound to the detergent-solubilized mouse MHC class II protein IE ^d has been studied by fluorescence techniques. Based on the efficiency of fluorescence quenching by the aqueous quenchers iodide and TEMPOL, different degrees of accessibility of the peptide-attached fluorescein moiety are distinguished in the lE^d-bound state, which depend on the nature of the peptide and on the site of attachment. These different extents of sequestration from the aqueous phase are reflected in the fluorescence properties of the corresponding NBD-labeled peptides bound to IE ^d. The results provide information on the topology of class II bound peptides.

【 授权许可】

Unknown