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

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...

Podrobná bibliografie
Hlavní autoři:	Reich, Z, Altman, J, Boniface, J, Lyons, D, Kozono, H, Ogg, G, Morgan, C, Davis, M
Médium:	Journal article
Jazyk:	English
Vydáno:	1997

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