Interaction between HLA-DMa and HLA-DR involves regions that undergo conformational changes at lysosomal pH

Interaction between HLA-DMa and HLA-DR involves regions that undergo conformational changes at lysosomal pH

The physical mechanism behind the catalytic activity of DM was investigated by using time-resolved fluorescence anisotropy and fluorescence binding studies with the dye 8-anilino-1-naphthalensulfonic acid.

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1997-11, Vol.94 (24), p.13163
Hauptverfasser: Ullrich, H Joachim, Doring, Klaus, Gruneberg, Ulrike, Jahnig, Fritz
Format: Artikel
Sprache:eng
Schlagworte:
Immunology
Molecular biology
Peptides
Proteins
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Zusammenfassung:The physical mechanism behind the catalytic activity of DM was investigated by using time-resolved fluorescence anisotropy and fluorescence binding studies with the dye 8-anilino-1-naphthalensulfonic acid.
ISSN:0027-8424
1091-6490