Signatures of co-translational folding.

Journal article

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: Saunders, R; Mann, M; Deane, C

• Publication status: Published
• Journal: Biotechnology journal
• Volume: 6
• Issue: 6
• Pages: 742-751
• Publication date: 2011-06-01
• DOI: 10.1002/biot.201000330
• EISSN: 1860-7314
• ISSN: 1860-6768
• Language: English
• Keywords: Protein Biosynthesis; Protein Conformation; Computational Biology; Protein Folding; Amino Acid Sequence; Ribosomes; Markov Chains; Algorithms; Models, Theoretical