Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module.
We have prepared a family of peptide fragments of the 64-residue chymotrypsin inhibitor 2, corresponding to its progressive elongation from the N terminus. The growing polypeptide chain has little tendency to form stable structure until it is largely synthesized, and what structures are formed are nonnative and lack, in particular, the native secondary structural elements of alpha-helix and beta-sheet. These elements then develop as sufficient tertiary interactions are made in the nearly full-length chain. The growth of structure in the small module is highly cooperative and does not result from the hierarchical accretion of substructures.
De Prat Gay
G
G
Medical Research Council Unit for Protein Function and Design, University of Cambridge, United Kingdom.
Ruiz-Sanz
J
J
Neira
J L
JL
Itzhaki
L S
LS
Fersht
A R
AR
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003488:Cyanogen Bromide; D004355:Drug Stability; D009682:Magnetic Resonance Spectroscopy; D008961:Models, Structural; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010446:Peptide Fragments / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D010940:Plant Proteins; D017354:Point Mutation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry
D010446:Peptide Fragments; D010455:Peptides; D010940:Plant Proteins; D011994:Recombinant Proteins; C093336:chymotrypsin inhibitor 2; D003488:Cyanogen Bromide