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
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Immunology
Molecular biology
Peptides
Proteins
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container_issue 24
container_start_page 13163
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 94
creator Ullrich, H Joachim
Doring, Klaus
Gruneberg, Ulrike
Jahnig, Fritz
description 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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ispartof Proceedings of the National Academy of Sciences - PNAS, 1997-11, Vol.94 (24), p.13163
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1091-6490
language eng
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source Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry
subjects Immunology
Molecular biology
Peptides
Proteins
title Interaction between HLA-DMa and HLA-DR involves regions that undergo conformational changes at lysosomal pH
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