title: Cotranslational protein folding--fact or fiction?
abstract: BACKGROUND
  Experimentalists have amassed extensive evidence over the past four decades that proteins appear to fold during production by the ribosome. Protein structure prediction methods, however, do not incorporate this property of folding. A thorough study to find the fingerprint of such sequential folding is the first step towards using it in folding algorithms, so assisting structure prediction.
  
  
  RESULTS
  We explore computationally the existence of evidence for cotranslational folding, based on large sets of experimentally determined structures in the PDB. Our perspective is that cotranslational folding is the norm, but that the effect is masked in most classes. We show that it is most evident in alpha/beta proteins, confirming recent findings. We also find mild evidence that older proteins may fold cotranslationally. A tool is provided for determining, within a protein, where cotranslation is most evident.
authors.affiliation: Department of Statistics, 1 South Park Road, Oxford University, Oxford OX1 3TG, UK.
authors.forename: Charlotte M
authors.initials: CM
authors.lastname: Deane
authors.forename: Mingqiang
authors.initials: M
authors.lastname: Dong
authors.forename: Fabien P E
authors.initials: FP
authors.lastname: Huard
authors.forename: Braddon K
authors.initials: BK
authors.lastname: Lance
authors.forename: Graham R
authors.initials: GR
authors.lastname: Wood
mesh_terms: D000595:Amino Acid Sequence; D003198:Computer Simulation; D030562:Databases, Protein; D008954:Models, Biological; D008956:Models, Chemical; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis / Q000502:physiology*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D020539:Sequence Analysis, Protein / Q000379:methods*; D012984:Software
chemical_list: D011506:Proteins