title: The folding and evolution of multidomain proteins.
abstract: Analyses of genomes show that more than 70% of eukaryotic proteins are composed of multiple domains. However, most studies of protein folding focus on individual domains and do not consider how interactions between domains might affect folding. Here, we address this by analysing the three-dimensional structures of multidomain proteins that have been characterized experimentally and observe that where the interface is small and loosely packed, or unstructured, the folding of the domains is independent. Furthermore, recent studies indicate that multidomain proteins have evolved mechanisms to minimize the problems of interdomain misfolding.
authors.affiliation: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
authors.forename: Jung-Hoon
authors.initials: JH
authors.lastname: Han
authors.forename: Sarah
authors.initials: S
authors.lastname: Batey
authors.forename: Adrian A
authors.initials: AA
authors.lastname: Nickson
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Teichmann
authors.forename: Jane
authors.initials: J
authors.lastname: Clarke
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000145:classification / Q000235:genetics*
chemical_list: D011506:Proteins