title: The intrinsically disordered C-RING biomineralization protein, AP7, creates protein phases that introduce nanopatterning and nanoporosities into mineral crystals.
abstract: We report an interesting process whereby the formation of nanoparticle assemblies on and nanoporosities within calcite crystals is directed by an intrinsically disordered C-RING mollusk shell nacre protein, AP7. Under mineralization conditions, AP7 forms protein phases that direct the nucleation of ordered calcite nanoparticles via a repetitive protein phase deposition process onto calcite crystals. These organized nanoparticles are separated by gaps or spaces that become incorporated into the forming bulk crystal as nanoporosities. This is an unusual example of organized nanoparticle biosynthesis and mineral modification directed by a C-RING protein phase.
authors: Laboratory for Chemical Physics, Department of Skeletal Biology, New York University , New York, New York 10012, United States.
authors: Eric P
authors: EP
authors: Chang
authors: Jennie A
authors: JA
authors: Russ
authors: Andreas
authors: A
authors: Verch
authors: Roland
authors: R
authors: Kröger
authors: Lara A
authors: LA
authors: Estroff
authors: John Spencer
authors: JS
authors: Evans
mesh_terms: D060105:Animal Shells / Q000737:chemistry*; D000818:Animals; D002113:Calcification, Physiologic; D003460:Crystallization; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D008974:Mollusca; D060734:Nacre / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D016062:Porosity
chemical_list: D064267:Intrinsically Disordered Proteins; D060734:Nacre