Co-translational folding.
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.
Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, TX 78712, USA. b.hardesty@mail.utexas.edu
B
B
Hardesty
T
T
Tsalkova
G
G
Kramer
D000595:Amino Acid Sequence; D018835:Chaperonin 10 / Q000378:metabolism; D018834:Chaperonin 60 / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism
D018835:Chaperonin 10; D018834:Chaperonin 60; D018832:Molecular Chaperones; D011506:Proteins