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Journal Article

Dynamical properties of fasciculin‐2


Helms,  Volkhard
Max Planck Research Group of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Baker, N. A., Helms, V., & McCammon, J. A. (1999). Dynamical properties of fasciculin‐2. Proteins: Structure, Function, and Bioinformatics, 36(4), 447-453. doi:10.1002/(SICI)1097-0134(19990901)36:4<447:AID-PROT8>3.0.CO;2-E.

Cite as: http://hdl.handle.net/21.11116/0000-0007-1DB1-1
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