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Free keywords:
fasciculin; acetylcholinesterase; molecular dynamics
Abstract:
Fasciculin‐2 (FAS2) is a potent protein inhibitor of the hydrolytic enzyme acetylcholinesterase. A 2‐ns isobaric‐isothermal ensemble molecular dynamics simulation of this toxin was performed to examine the dynamic structural properties which may play a role in this inhibition. Conformational fluctuations of the FAS2 protein were examined by a variety of techniques to identify flexible residues and determine their characteristic motion. The tips of the toxin “finger” loops and the turn connecting loops I and II were found to fluctuate, while the rest of the protein remained fairly rigid throughout the simulation. Finally, the structural fluctuations were compared to NMR data of fluctuations on a similar timescale in a related three‐finger toxin. The molecular dynamics results were in good qualitative agreement with the experimental measurements
