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Modeling and simulation of ion-coupled and ATP-driven membrane proteins

MPG-Autoren
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Faraldo-Gómez,  Jóse D.
Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Forrest,  Lucy R.
Max Planck Research Group of Computational Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Faraldo-Gómez, J. D., & Forrest, L. R. (2011). Modeling and simulation of ion-coupled and ATP-driven membrane proteins. Current Opinion in Structural Biology, 21(2), 173-179.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-D5F6-D
Zusammenfassung
The molecular mechanisms of membrane proteins that are activated either by ions or by ATP are just beginning to come into focus, as long-awaited structural data are revealed. This information is being leveraged and supplemented to great effect by molecular modeling and computer simulation studies. Important examples include the homology modeling of eukaryotic protein structures based on distantly related templates, as well as the use of internal structural symmetry for modeling different states in conformational cycles. Molecular simulation studies have elucidated the location and coordination structure of ion binding sites, and explained their selectivity, while also providing tantalizing insights into the mechanisms that couple conformational change to ion translocation or ATP hydrolysis.