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PMID: 7731965 Published · ppublish English Comparative Study Journal Article

Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 92 ·No. 9 ·1995-04-25 ·Pages 3683-6

De Prat Gay G, Ruiz-Sanz J, Neira JL, Itzhaki LS, Fersht AR

Abstract

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.

MeSH Terms
Amino Acid Sequence Circular Dichroism Cyanogen Bromide Drug Stability Magnetic Resonance Spectroscopy Models, Structural Molecular Sequence Data Mutagenesis, Site-Directed Peptide Fragments/chemistry Peptides/chemistry,genetics Plant Proteins Point Mutation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins/chemistry
Chemicals
Peptide Fragments Peptides Plant Proteins Recombinant Proteins chymotrypsin inhibitor 2 Cyanogen Bromide
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
De Prat Gay G
Medical Research Council Unit for Protein Function and Design, University of Cambridge, United Kingdom.
Ruiz-Sanz J
Neira J L
Itzhaki L S
Fersht A R
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.92.9.3683
Published
1995-04-25
Pages
3683-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC42025
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.92.9.3683 PMC Full Text View journal details
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