title: Signatures of co-translational folding.
abstract: Global and co-translational protein folding may both occur in vivo, and understanding the relationship between these folding mechanisms is pivotal to our understanding of protein-structure formation. Within this study, over 1.5 million hydrophobic-polar sequences were classified based on their ability to attain a unique, but not necessarily minimal energy conformation through co-translational folding. The sequence and structure properties of the sets were then compared to elucidate signatures of co-translational folding. The strongest signature of co-translational folding is a reduced number of possible favorable contacts in the amino terminus. There is no evidence of fewer contacts, more local contacts, or less-compact structures. Co-translational folding produces a more compact amino- than carboxy-terminal region and an amino-terminal-biased set of core residues. In real proteins these signatures are also observed and found most strongly in proteins of the alpha/beta structural class of proteins (SCOP) where 71 % have an amino-terminal set of core residues. The prominence of co-translational features in experimentally determined protein structures suggests that the importance of co-translational folding is currently underestimated.
authors.affiliation: Oxford University, Department of Statistics, Oxford, UK.
authors.forename: Rhodri
authors.initials: R
authors.lastname: Saunders
authors.forename: Martin
authors.initials: M
authors.lastname: Mann
authors.forename: Charlotte M
authors.initials: CM
authors.lastname: Deane
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D019295:Computational Biology / Q000379:methods; D008390:Markov Chains; D008962:Models, Theoretical; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017510:Protein Folding; D012270:Ribosomes / Q000502:physiology