title: Protein folding by interaction.
abstract: Repeat proteins consisting of helical segments seem to fold by a matrix-assisted mechanism in which folded segments induce structure in intrinsically disordered parts of the protein, as shown by Watson and colleagues in this issue of Structure for an Armadillo repeat protein and previously by the Balbach group for an Ankyrin repeat protein.
authors.affiliation: Center of Integrated Protein Science, Department Chemie, Technische Universität München, 80333 München, Germany. Electronic address: johannes.buchner@tum.de.
authors.forename: Johannes
authors.initials: J
authors.lastname: Buchner
authors.affiliation: Center of Integrated Protein Science, Department Chemie, Technische Universität München, 80333 München, Germany; Institute for Advanced Study, Technische Universität München, 80333 München, Germany; Chemistry Department, Faculty of Sciences, King Abdulaziz University, Jeddah 22254, Saudi Arabia. Electronic address: kessler@tum.de.
authors.forename: Horst
authors.initials: H
authors.lastname: Kessler
mesh_terms: D000818:Animals; D051186:Armadillo Domain Proteins / Q000737:chemistry*; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D051186:Armadillo Domain Proteins; D010446:Peptide Fragments