Co-translational folding

Curr Opin Struct Biol. 1999 Feb;9(1):111-4. doi: 10.1016/s0959-440x(99)80014-1.

Abstract

Nascent proteins appear to fold co-translationally. The ribosome itself may function as a chaperone, providing a sheltered environment in which the nascent peptide is protected from aggregation and degradation, and in which folding into the tertiary structure is facilitated by interactions both with ribosomal proteins and with specific segments of the ribosomal RNA.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Chaperonin 10 / metabolism
  • Chaperonin 60 / metabolism
  • Molecular Chaperones / metabolism
  • Protein Biosynthesis*
  • Protein Conformation
  • Protein Folding*
  • Proteins / chemistry*
  • Proteins / genetics*
  • Proteins / metabolism
  • Ribosomes / metabolism

Substances

  • Chaperonin 10
  • Chaperonin 60
  • Molecular Chaperones
  • Proteins