Stability of empty and peptide-loaded class II major histocompatibility complex molecules at neutral and endosomal pH: Comparison to class I proteins

The structure and thermal stability of empty and peptide-filled forms of the murine class II major histocompatibility complex (MHC) molecule I-E(k) were studied at neutral and mildly acidic pH. The two forms have distinct circular dichroic spectra, suggesting that a conformational change may accompa...

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Autores principales: Reich, Ziv, Altman, John D., Boniface, J. Jay, Lyons, Daniel S., Kozono, Haruo, Ogg, Graham, Morgan, Chantal, Davis, Mark M.
Formato: Artigo
Lenguaje:Inglês
Publicado: The National Academy of Sciences of the USA 1997
Materias:
Biological Sciences
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC20116/
https://ncbi.nlm.nih.gov/pubmed/9122223
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