Sandbox FIg 5b

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page Sandbox FIg 5b. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function 009 Fig 5b_png 009 Fig 5b_png_created_with_default_jmol Disease xyz_off an between them. The stability of the 4D motif is attributed to adjacent positively charged residues (Lys325, Arg388, and Arg517), forming stabilizing salt bridges, leading to the newly named 4A/3B motif (four acidic residues stabilized by three basic residues). The study also identified additional metal-binding sites (His264 and His471 sites) in TcAChE through crystallographic analysis, but these appear to be weaker or crystallographic artifacts. Using metadynamics and molecular dynamics (MD) simulations with quantum potentials (QM/MM-MD), the binding strength of metal cations at the 4D site was compared to that of the 4D site in human fibrin-stabilizing factor (fXIIIa), which lacks stabilizing cationic residues. Results showed that while TcAChE’s 4A/3B motif maintains structural integrity upon metal binding/unbinding, the fXIIIa motif is stable in presence of a metal ion but explodes without a metal ions due to electrostatic repulsion. This is seen clearly in an between these two states. Structural highlights This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.