Model of a full-sized antibody (IgG) bound to two molecules of the designed binder () at its Fc-domain. Close-up inset shows the interactions between the normally surface-exposed histidine residue (His433) of the IgG with the binder. Switching takes place from the high-affinity binding at higher pH (pH ) when the histidine is not protonated to a much lower affinity binding at lower pH (pH ) when the histidine becomes protonated. (Image courtesy: Dr. David Baker, University of Washington) Computer-designed binding protein could lead to better protection for our Warfighters 140224-A-

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Model of a full-sized antibody (IgG) bound to two molecules of the designed binder () at its Fc-domain. Close-up inset shows the interactions between the normally surface-exposed histidine residue (His433) of the IgG with the binder. Switching takes place from the high-affinity binding at higher pH (pH ) when the histidine is not protonated to a much lower affinity binding at lower pH (pH ) when the histidine becomes protonated. (Image courtesy: Dr. David Baker, University of Washington) Computer-designed binding protein could lead to better protection for our Warfighters 140224-A-AB123-003

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Photo credit: © PJF Military Collection / Alamy / Afripics
License: Licensed
Model Released: No

Keywords: armed, cb, conflict, dtra, forces, military, states, united, war