Pressure jump is known to induce fast protein folding. For a five-helix bundle ?-repressor frag- ment, a short refolding time of ~2 �s was reported in an earlier pressure-jump experiment. To investigate this pressure-jump induced fast folding behavior, all-atom molecular dynamics simulations of more than 33 �s in explicit solvent were carried out on the same ?-repressor con- struct. High-pressure denatured states, generated through a high-temperature unfolding and high-pressure equilibration simulation procedure, were found to contain a significant amount of helical structure. Upon pressure drop, the protein refolded into the native state in 20 �s. The folding in the simulation is slower than the one measured in pressure-jump experiment, but faster than the folding time of 80 �s measured in temperature-jump experiment. A complete unfolding and refolding process was observed in the trajectory, which permitted the characteri- zation of high-pressure denatured states and refolding pathway. The pressure jump simulations carried out for this study can be employed in the future to investigate slow-folding proteins through 10~100 �s molecular dynamics simulations by inducing a fast folding phase.

Fast protein refolding observed in pressure-jump molecular dynamics simulation

245th National Meeting (2013)

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