Femtosecond study of partially folded states of cytochrome C by solvation dynamics

Study is conducted using femtosecond time-resolved fluorescence spectroscopy, to show that the solvation dynamics in the two partially folded states (I(sub s)(super ') and I(sub s)(super '') of a protein, cytochrome C, are very different. Solvation dynamics of I(sub s)(super '') displays a major component of 1.3 ps which indicates that the structure of I(sub s)(super '') is much more open and exposed compared to that of I(sub s)(super ').