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Published December 4, 1992 | public
Journal Article

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

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.

Additional Information

© 1992 American Association for the Advancement of Science. Received 1 July 1992, accepted 2 October 1992. We thank M. Raghavan for doing the acid-elution experiments, D. C. Rees and T. Arakawa for helpful discussions, C. Bebbington for the glutamine synthetase amplification vector; J. Moore for help with CD analysis, D. Penny tor assistance with tissue culture, M. Blum and R. Strong for help with graphics, and D. C. Rees, N. Davidson, and M. Raghavan for critical reading of the manuscript Supported by NIH (Al28931 to P.J.B.), and an NIH postdoctoral fellowship (M.L.F.). P.J.B is a scholar of the Pew Charitable Trusts and the Cancer Research Institute.

Additional details

Created:
August 20, 2023
Modified:
October 18, 2023