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The accessibility of peptides bound to the mouse MHC class II molecule IEd studied by fluorescence
1Department of Chemistry, Stanford University, CA 94305.
The accessibility of fluorescently labeled (antigenic) peptides bound to the detergent-solubilized mouse MHC class II protein IEd 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 IEd-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 IEd. The results provide information on the topology of class II bound peptides.
The accessibility of fluorescently labeled (antigenic) peptides bound to the detergent-solubilized mouse MHC class II protein IEd 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 IEd-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 IEd. The results provide information on the topology of class II bound peptides.