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- W2035937996 abstract "A secreted form of a class I major histocompatibility complex (MHC) molecule was denatured and renatured in vitro in the absence of peptide. The resulting empty class I heterodimer was immunologically reactive and structurally similar to a heterodimer renatured in the presence of an appropriate restricted peptide. Thermal stability profiles indicated that the two forms of heterodimer differed in their resistance to denaturation by heat but that a significant portion of the empty class I heterodimers had a native conformation at physiological temperatures. Free energies calculated from these data gave a direct measure of the stabilization of the class I MHC molecule that resulted from peptide binding." @default.
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- W2035937996 date "1992-12-04" @default.
- W2035937996 modified "2023-09-26" @default.
- W2035937996 title "Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule" @default.
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- W2035937996 doi "https://doi.org/10.1126/science.1360705" @default.
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