title: Dynamical properties of fasciculin-2.
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.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093-0365, USA. nbacker@wasabi.ucsd.edu
authors.forename: N A
authors.initials: NA
authors.lastname: Baker
authors.forename: V
authors.initials: V
authors.lastname: Helms
authors.forename: J A
authors.initials: JA
authors.lastname: McCammon
mesh_terms: D000818:Animals; D002800:Cholinesterase Inhibitors / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D004546:Elapid Venoms / Q000737:chemistry* / Q000378:metabolism*; D017815:Elapidae; D006860:Hydrogen Bonding; D007700:Kinetics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012984:Software; D012997:Solvents; D013816:Thermodynamics
chemical_list: D002800:Cholinesterase Inhibitors; D004546:Elapid Venoms; D012997:Solvents; C044937:fasciculin