@Article{SaundersMann_11,
  author = 	 {Rhodri Saunders and Martin Mann and Charlotte Deane},
  title = 	 {Signatures of Co-translational Folding},
  journal = 	 {Biotechnology Journal, Special issue: Protein folding in vivo},
  issn = 	 {1860-7314},
  year = 	 {2011},
  volume = 	 {6},
  number = 	 {6},
  pages = 	 {742-751},
  doi = 	 {10.1002/biot.201000330},
  month = 	 {March},
  user = 	 {mmann},
  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 via 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 favourable contacts in the amino-terminus. There is no evidence of fewer contacts, more local contacts, nor less compact structures. Co-translational folding does produce 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 SCOP alpha/beta class 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.},
  note =	 {RS and MM have contributed equally to this work.}
}