A multibaric-multithermal molecular dynamics (MD) simulation of a 10-residue protein, chignolin was performed to study its folding and unfolding thermodynamics and the denaturation mechanisms. This MD simulation covered wide ranges of temperature between T= 260 � 560 K and pressure between P= 0.1 � 600 MPa and sampled many conformations without getting trapped in local-minimum free-energy states. Folding events to the native beta-hairpin structure occurred five times and unfolding events were observed four times. As temperature and/or pressure increases, fraction of the folded chignolin decreases. The partial molar enthalpy change and partial molar volume change upon unfolding were calculated and these values agree well with recent experimental results. Illustrating typical local-minimum free-energy conformations, folding and unfolding pathways of the chignolin were also revealed.

Temperature and pressure denaturation of chignolin: Folding and unfolding simulation by multibaric-multithermal molecular dynamics algorithm

243rd National Meeting (2012)

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