Structural characterization and unfolding mechanism of human 4F2hc ectodomain

► 4F2hc-ED is monomeric, highly compact and stable, with buried Trp residues ► Urea unfolding equilibrium reveals two intermediate states ► I1 state resembles a highly structured molten globule ►I2 state is mainly unstructured but with strong hydrophobic interactions ►Folding is probably initiated by formation of hydrophobic clusters