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Vol 45(2011) N 6 p. 976-982;
V.M. Tishchenko*

Unusual Thermodynamic Properties of a Compact State of IgG3 Kuc and Sur pFh Fragments (Hinge Region)

Institute of Biological Instrumentation Russian Academy of Science, Pushchino, Moscow Region, Pushchino, 142290 Russia

*tischen@vega.protres.ru
Received - 2010-09-06; Accepted - 2011-04-05

The pFh fragments from the hinge region of human IgG3 Kuc and Sur are able to fold into a compact structure, thereby giving proteins with secondary (supersecondary) structure, mainly represented by the left-handed polyproline II helix. It has been shown that thermal denaturation of a compact pFh from the hinge region of IgG3 Kuc and Sur comprises two stages. At the first stage, the compact protein structure unfolds according to the all-or-none model with retention of the secondary structure. At the second stage, the lefthanded polyproline II helix, composed of four separate cooperative blocks formed of strands with a high content of proline residues, melts itself. A polyproline conformation of the secondary structure and alarge number of disulfide bonds between the chains determine a high specific enthalpy of denaturation and a high thermal stability, respectively.

pFh fragment, double poly-L-proline helix, cooperative units, tertiary structure



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