title: Enzyme nanorings.
abstract: We have demonstrated that nanostructures, and in particular nanorings incorporating a homodimeric enzyme, can be prepared by chemically induced self-assembly of dihydrofolate reductase (DHFR)-histidine triad nucleotide binding 1 (Hint1) fusion proteins. The dimensions of the nanorings were found by static light scattering and atomic force microscopy studies to be dependent on the length and composition of the peptide linking the fusion proteins, ranging in size from 10 to 70 nm in diameter and 64 to 740 kDa. The catalytic efficiency of the nanorings was found to be dependent on ring size, thus suggesting that the arrangement of supermolecular assemblies of enzymes may be used to control their catalytic parameters.
authors.affiliation: Department of Medicinal Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.
authors.forename: Tsui-Fen
authors.initials: TF
authors.lastname: Chou
authors.forename: Christopher
authors.initials: C
authors.lastname: So
authors.forename: Brian R
authors.initials: BR
authors.lastname: White
authors.forename: Jonathan C T
authors.initials: JC
authors.lastname: Carlson
authors.forename: Mehmet
authors.initials: M
authors.lastname: Sarikaya
authors.forename: Carston R
authors.initials: CR
authors.lastname: Wagner
mesh_terms: D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry*; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry*
chemical_list: C063306:HINT1 protein, human; D009419:Nerve Tissue Proteins; D013762:Tetrahydrofolate Dehydrogenase