Abstract
The Fc fragment of human IgG1 can be trapped in a stable intermediate state during thermal denaturation. In this conformation the molecule is compact with a native-like secondary structure, however, the tertiary structure is perturbed as revealed by intrinsic fluorescence measurements, the near-UV CD spectra and by mapping of antigenic sites with monoclonal antibodies. Similar phenomena were recently described for a few globular proteins of small size, and termed ‘the molten globule’ state. Our observation is a unique example of this phenomenon for a four domain protein.
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