Unbiased simulation of structural transitions in calmodulin

Details Unbiased simulation of structural transitions in calmodulin Unbiased simulation of structural transitions in calmodulin

2003-02-28

arxiv.org/abs/physics/0302103v1

Physics

Biological Physics

Scientific paper

We 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.

Affiliated with

Also associated with

No associations

Rating

Unbiased simulation of structural transitions in calmodulin does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Unbiased simulation of structural transitions in calmodulin, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Unbiased simulation of structural transitions in calmodulin will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-643720