Folding at the birth of the nascent chain: coordinating translation with co-translational folding

Curr Opin Struct Biol. 2011 Feb;21(1):25-31. doi: 10.1016/ Epub 2010 Nov 24.


In the living cells, the folding of many proteins is largely believed to begin co-translationally, during their biosynthesis at the ribosomes. In the ribosomal tunnel, the nascent peptide may establish local interactions and stabilize α-helical structures. Long-range contacts are more likely outside the ribosomes after release of larger segments of the nascent chain. Examples suggest that domains can attain native-like structure on the ribosome with and without population of folding intermediates. The co-translational folding is limited by the speed of the gradual extrusion of the nascent peptide which imposes conformational restraints on its folding landscape. Recent experimental and in silico modeling studies indicate that translation kinetics fine-tunes co-translational folding by providing a time delay for sequential folding of distinct portions of the nascent chain.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Protein Biosynthesis*
  • Protein Folding*
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Proteins / genetics
  • Proteins / metabolism*
  • RNA, Messenger / genetics
  • Ribosomes / chemistry
  • Ribosomes / metabolism


  • Proteins
  • RNA, Messenger