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Science 4 December 1992:
Vol. 258. no. 5088, pp. 1658 - 1662
DOI: 10.1126/science.1360705
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Articles

Science, Vol 258, Issue 5088, 1658-1662
Copyright © 1992 by American Association for the Advancement of Science

articles

Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule

ML Fahnestock, I Tamir, L Narhi, and PJ Bjorkman

Division of Biology, California Institute of Technology, Pasadena 91125.

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.


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