The stability of CopC, a copper resistant protein with a Greek β-barrel motif, in GuHCl solution was investigated by fluorescence spectra. Parameter A, characterizing position and shape of the fluorescence spectra, "phase diagram" method of fluorescence, and cupric binding capacity in GuHCl solution of different concentration showed that the denaturation transition of apo-CopC and CopC-Cu(II) might be fitted to a simple two-state model. According to a two-state model, the free energy of stabilization for apo-CopC and CopC-Cu(II), (17.08±0.35) and (23.81±0.45) kJ•mol -1 respectively, was obtained. Copper(II) increased the stability of apo-CopC. The higher thermodynamics stability of CopC-Cu(II) was revealed to originate in both the faster folding and the slower unfolding rates by unfolding kinetics.