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The accessibility of peptides bound to the mouse MHC class II molecule IE d studied by fluorescence
Author(s) -
de Kroon Anton I.P.M.
Publication year - 1994
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 - 10.1016/0014-5793(94)80507-5
Subject(s) - fluorescence , chemistry , peptide , moiety , mhc class i , quenching (fluorescence) , iodide , molecule , stereochemistry , major histocompatibility complex , biophysics , biochemistry , biology , organic chemistry , physics , quantum mechanics , gene
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.