Denaturation properties and folding transition states of leghemoglobin and other heme proteins

摘要: This work reports unfolding transitions of monomeric heme proteins leghemoglobin (Lb), myoglobin (Mb), and cytochrome c (Cyt c) utilizing UV-Vis spectra, steady-state time-resolved fluorescence methods. Conformational stabilities the native “folded” state their “unfolded” states were investigated in light a two-state transition model. Two-state values for ΔGD (298K) obtained by denaturation with chaotropic agents urea guanidium hydrochloride (GdnHCl). The free energy value Lb is lowest compared to Cyt Mb along pathway. m also Mb. (a measure dependence on denaturant concentration) lower when it denatured GdnHCl. absorbance maximum steady emission drastically red shifted presence certain concentration both cases Lb, but scenario different c. results are analyzed using lifetime data clearly indicate an intermediate during denaturation. can modulate conformation, stability, surface exposure these biologically important proteins.