volume 32, issue 44, P11761-11768 1993
DOI: 10.1021/bi00095a003
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J. Jay Boniface, Nancy L. Allbritton, Philip A. Reay, Ronald M. Kantor, Lubert Stryer, Mark M. Davis

Abstract: We have compared the contribution of electrostatic forces in the binding of antigenic peptides to the class II MHC molecule, IEk, at weakly acidic (pH 5.4) and neutral (pH 7.5) pH values. The binding of specific moth cytochrome c (MCC) and hemoglobin (Hb) peptides to IEk is very sensitive to ionic strength at pH 7.5 but not at pH 5.4, indicating that the mechanism of peptide binding is pH-dependent. Substitution of the C-terminal Lys in MCC for an Ala residue selectively destroyed peptide binding at neutral pH…

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