Unbiased simulation of structural transitions in calmodulin

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dc.creatorZuckerman, Daniel M.
dc.date2003-02-28
dc.date.accessioned2026-07-07T05:48:51Z
dc.date.available2026-07-07T05:48:51Z
dc.descriptionWe introduce an approach for performing "very long" computer simulations of the dynamics of simplified, folded proteins. Using an alpha-carbon protein model and a fine grid to mimic continuum computations at increased speed, we perform unbiased simulations which exhibit many large-scale conformational transitions at low cost. In the case of the 72-residue N-terminal domain of calmodulin, the approach yields structural transitions between the calcium-free and calcium-bound structures at a rate of roughly one per day on a single Intel processor. Stable intermediates can be clearly characterized. The model employs Go-like interactions to stabilize two (or more) experimentally-determined structures. The approach is trivially parallelizable and readily generalizes to more complex potentials at minimal cost.
dc.identifierhttps://arxiv.org/abs/physics/0302103
dc.identifierhttp://arxiv.org/abs/physics/0302103
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/85183
dc.subjectBiological Physics
dc.subjectChemical Physics
dc.subjectComputational Physics
dc.subjectQuantitative Biology
dc.titleUnbiased simulation of structural transitions in calmodulin
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