Abstract: We used molecular dynamics (MD) method based on OPLS-AA (optimized potentials for liquid simulations all atom) force field to investigate the hydrophobic properties of cysteine-rich protein from soybean and  the weak interactions between protein and solvent,  and   studied  the free energy changes of the protein at different λ from the aspects of  thermodynamics and  dynamics. The results show that the cysteine has a decisive effect on the protein properties,  and the solvent  mainly affects  the protein conformations. 

Key words: soybean,  , cysteine-rich protein,  , molecular dynamics,  , free energy