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dc.contributor.advisorBaker, David
dc.contributor.authorPyles, Harley
dc.date.accessioned2019-10-15T23:00:10Z
dc.date.submitted2019
dc.identifier.otherPyles_washington_0250E_20663.pdf
dc.identifier.urihttp://hdl.handle.net/1773/44861
dc.descriptionThesis (Ph.D.)--University of Washington, 2019
dc.description.abstractProteins that interface with inorganic crystals have critical functions in biology. For example, biomineralization proteins form hard tissues such as bone, abalone shell, and sponge spicules, and mineral binding proteins in iron-reducing bacteria transfer electrons to their environment. While the atomistic details of natural protein-mineral interfaces remain largely unknown, inspiration for design can be gleaned from ice-binding proteins that display arrays of amino-acid side-chains spaced in regular intervals that geometrically match the ice lattice surface. Collaborators and I hypothesized that a similar lattice-matching approach could be used to design interactions between proteins and minerals. Using designed-helical repeat proteins engineered to adsorb and assemble on the mica (001) surface, we demonstrated this approach can control protein assembly on the surface of an inorganic crystal.
dc.format.mimetypeapplication/pdf
dc.language.isoen_US
dc.rightsnone
dc.subjectAtomic force microscopy
dc.subjectComputational protein design
dc.subjectProtein-mineral interface
dc.subjectBiochemistry
dc.subjectBiophysics
dc.subject.otherMolecular and cellular biology
dc.titleControlling protein assembly on mineral surface with designed interfaces
dc.typeThesis
dc.embargo.termsRestrict to UW for 1 year -- then make Open Access
dc.embargo.lift2020-10-14T23:00:10Z


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