1981 · 84 citations · 12 references
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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S. M. Ibrahim Shah · 1977 · 376 citations
MONOPHYLY OR DIPHYLY IN THE ORIGIN OF WHALES
Leigh Van Valen · Evolution · 1968 · 79 citations
Stratigraphy of the Kohat Quadrangle, Pakistan
Charles R. Meissner, J.M. Master, Mohammad Mamun Ur Rashid et al. · USGS professional paper · 1974 · 78 citations · Full text