title: Ring and zipper formation is the key to understanding the structural variety in all-beta proteins.
abstract: A novel structural classification of beta proteins is presented from the viewpoint of the ring-shaped structure and the zipper-like contact pattern, based on the fact that 92% and 60% of beta proteins have the ring topology and the zippered contact pattern, respectively. We discuss the implication of the unexpectedly high preference for the ring and zippered structures in connection with the folding process of beta proteins.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Kitashirakawa-Oiwake-cho, Sakyo-ku, Kyoto, 606-8502, Japan. kioke@tsurumi.yokohama-cu.ac.jp
authors.forename: Ryotaro
authors.initials: R
authors.lastname: Koike
authors.forename: Kengo
authors.initials: K
authors.lastname: Kinoshita
authors.forename: Akinori
authors.initials: A
authors.lastname: Kidera
mesh_terms: D008958:Models, Molecular; D015394:Molecular Structure; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins