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Biophys J, July 2002, p. 98-111, Vol. 83, No. 1

Orientation and Conformation of a Lipase at an Interface Studied by Molecular Dynamics Simulations

Morten Ø. Jensen,* Torben R. Jensen,dagger Kristian Kjaer,Dagger Thomas Bjørnholm,§ Ole G. Mouritsen, and Günther H. Peters*

 *Center for Biomembrane Physics (MEMPHYS), Department of Chemistry, Technical University of Denmark, DK-2800 Lyngby, Denmark;  dagger Department of Chemistry, University of Aarhus, DK-8000 Århus C, Denmark;  Dagger Condensed Matter Physics and Chemistry Department, Risø National Laboratory, DK-4000 Roskilde, Denmark;  §Nano-Science Center, Chemistry Department, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen Ø, Denmark; and  Center for Biomembrane Physics (MEMPHYS), Physics Department, University of Southern Denmark, DK-5230 Odense M, Denmark

Electron density profiles calculated from molecular dynamics trajectories are used to deduce the orientation and conformation of Thermomyces lanuginosa lipase and a mutant adsorbed at an air-water interface. It is demonstrated that the profiles display distinct fine structures, which uniquely characterize enzyme orientation and conformation. The density profiles are, on the nanosecond timescale, determined by the average enzyme conformation. We outline a computational scheme that from a single molecular dynamics trajectory allows for extraction of electron density profiles referring to different orientations of the lipase relative to an implicit interface. Profiles calculated for the inactive and active conformations of the lipase are compared with experimental electron density profiles measured by x-ray reflectivity for the lipase adsorbed at an air-water interface. The experimental profiles contain less fine structural information than the calculated profiles because the resolution of the experiment is limited by the intrinsic surface roughness of water. Least squares fits of the calculated profiles to the experimental profiles provide areas per adsorbed enzyme and suggest that Thermomyces lanuginosa lipase adsorbs to the air-water interface in a semiopen conformation with the lid oriented away from the interface.

Biophys J, July 2002, p. 98-111, Vol. 83, No. 1
© 2002 by the Biophysical Society   0006-3495/02/07/98/14  $2.00


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Reorientational Dynamics of Enzymes Adsorbed on Quartz: A Temperature-Dependent Time-Resolved TIRF Anisotropy Study
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