Dynamical properties of fasciculin-2
N A Baker1, V Helms, J A McCammon
1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093-0365, USA. nbacker@wasabi.ucsd.edu
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. Proteins 1999;36:447-453.
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