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Biochemistry. 2011 Feb 15;50(6):981-8. doi: 10.1021/bi101549n. Epub 2011 Jan 24.

Thermal induction of an alternatively folded state in human IgG-Fc.

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  • 1Division of Molecular Physics, Department of Physics, Linköping University, SE-581 83 Linköping, Sweden.

Abstract

We report the formation of a non-native, folded state of human IgG4-Fc induced by a high temperature at neutral pH and at a physiological salt concentration. This structure is similar to the molten globule state in that it displays a high degree of secondary structure content and surface-exposed hydrophobic residues. However, it is highly resistant to chemical denaturation. The thermally induced state of human IgG4-Fc is thus associated with typical properties of the so-called alternatively folded state previously described for murine IgG, IgG-Fab, and individual antibody domains (V(L), V(H), C(H)1, and C(H)3) under acidic conditions in the presence of anions. Like some of these molecules, human IgG4-Fc in its alternative fold exists as a mixture of different oligomeric structures, dominated by an equilibrium between monomeric and heptameric species. Heating further induces the formation of fibrous structures in the micrometer range.

PMID:
21261247
[PubMed - indexed for MEDLINE]
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