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Originally published In Press as doi:10.1074/jbc.M301086200 on February 9, 2003

J. Biol. Chem., Vol. 278, Issue 17, 14732-14738, April 25, 2003
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Thermodynamic Analysis of the Increased Stability of Major Histocompatibility Complex Class II Molecule I-Ek Complexed with an Antigenic Peptide at an Acidic pH*

Keigo SaitoDagger , Akinori Sarai§, Masayuki OdaDagger , Takachika AzumaDagger , and Haruo KozonoDagger

From the Dagger  Research Institute for Biological Sciences (RIBS), Tokyo University of Science, 2669, Yamazaki, Noda, Chiba 278-0022, Japan and the § Tsukuba Institute, Institute of Physical and Chemical Research (RIKEN), Tsukuba, Ibaraki 305-0077, Japan

The differential scanning calorimetry analysis of the murine major histocompatibility complex class II molecule, I-Ek, in complex with an antigenic peptide derived from mouse hemoglobin, showed that the thermal stability at the mildly acidic pH is higher than that at the neutral pH. Although the thermal unfolding of I-Ek-hemoglobin was irreversible, we extracted the equilibrium thermodynamic parameters from the kinetically controlled heat capacity curves. Both the denaturation temperatures and the enthalpy changes were almost independent of the heating rate over 1 °C per min. The linear relation between the denaturation temperature and the calorimetric enthalpy change provided the heat capacity changes, which are classified into one for the mildly acidic pH region and another for the neutral pH region. The equilibrium thermodynamic parameters showed that the increased stability at the mildly acidic pH is because of the entropic effect. These thermodynamic data provided new insight into the current structural model of a transition to an open conformation at the mildly acidic pH, which is critical for the peptide exchange function of major histocompatibility complex class II in the endosome.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 81-4-7123-9937; Fax: 81-4-7124-1541; E-mail: kozonoh@rs.noda.tus.ac.jp.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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