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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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| Hlavní autoři: | , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
The National Academy of Sciences of the USA
1997
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC20116/ https://ncbi.nlm.nih.gov/pubmed/9122223 |
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