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Mechanical unfolding of the fourth domain of Distyostelium discoideum filamin(DDFLN4) was studied by all-atom molecular dynamics simulations, using theGROMOS96 force field 43a1 and the simple point charge explicit water solvent.Our study reveals an important role of non-native interactions in the unfoldingprocess. Namely, the existence of a peak centered at the end-to-end extension22 nm in the force-extension curve, is associated with breaking of non-nativehydrogen bonds. Such a peak has been observed in experiments but not in Gomodels, where non-native interactions are neglected. We predict that anadditional peak occurs at 2 nm using not only GROMOS96 force field 43a1 butalso Amber 94 and OPLS force fields. This result would stimulate furtherexperimental studies on elastic properties of DDFLN4.

Protein mechanical unfolding: importance of non-native interactions