title: Design and characterization of a homodimeric antiparallel coiled coil.
abstract: We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications.
authors.affiliation: Department of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405-7102, USA.
authors.forename: Daniel G
authors.initials: DG
authors.lastname: Gurnon
authors.forename: Jennifer A
authors.initials: JA
authors.lastname: Whitaker
authors.forename: Martha G
authors.initials: MG
authors.lastname: Oakley
mesh_terms: D002942:Circular Dichroism; D019281:Dimerization; D057927:Hydrophobic and Hydrophilic Interactions; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins