A 'molten globule'-like unfolding intermediate of a four domain protein, the Fc fragment of the IgG molecule.
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.
Vonderviszt
F
F
Institute of Enzymology, Hungarian Academy of Sciences, Budapest.
Lakatos
S
S
Gál
P
P
Sárvári
M
M
Závodszky
P
P
D000911:Antibodies, Monoclonal; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D006801:Humans; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G / Q000302:isolation & purification; D007700:Kinetics; D009101:Multiple Myeloma / Q000276:immunology; D011487:Protein Conformation; D011489:Protein Denaturation
D000911:Antibodies, Monoclonal; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G