Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Fersht, A., Itzhaki, L., Elmasry, N., Matthews, J., & Otzen, D. Proceedings of the National Academy of Sciences of the United States of America, 91(22):10426-10429, 1994. cited By 169![Single versus parallel pathways of protein folding and fractional formation of structure in the transition state [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Protein engineering and kinetic experiments indicate that some regions of proteins have partially formed structure in the transition state for protein folding. A crucial question is whether there is a genuine single transition state that has interactions that are weakened in those regions or there are parallel pathways involving many transition states, some with the interactions fully formed and others with the structural elements fully unfolded. We describe a kinetic test to distinguish between these possibilities. The kinetics rule out those mechanisms that involve a mixture of fully formed or fully unfolded structures for regions of the barley chymotrypsin inhibitor 2 and barnase, and so those regions are genuinely only partially folded in the transition state. The implications for modeling of protein folding pathways are discussed.
@ARTICLE{Fersht199410426,
author={Fersht, A.R. and Itzhaki, L.S. and Elmasry, N.F. and Matthews, J.M. and Otzen, D.E.},
title={Single versus parallel pathways of protein folding and fractional formation of structure in the transition state},
journal={Proceedings of the National Academy of Sciences of the United States of America},
year={1994},
volume={91},
number={22},
pages={10426-10429},
doi={10.1073/pnas.91.22.10426},
note={cited By 169},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028037217&doi=10.1073%2fpnas.91.22.10426&partnerID=40&md5=30cf24d57681d64e4821e72e03f96a26},
affiliation={Cambridge Ctr. for Protein Eng., Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom},
abstract={Protein engineering and kinetic experiments indicate that some regions of proteins have partially formed structure in the transition state for protein folding. A crucial question is whether there is a genuine single transition state that has interactions that are weakened in those regions or there are parallel pathways involving many transition states, some with the interactions fully formed and others with the structural elements fully unfolded. We describe a kinetic test to distinguish between these possibilities. The kinetics rule out those mechanisms that involve a mixture of fully formed or fully unfolded structures for regions of the barley chymotrypsin inhibitor 2 and barnase, and so those regions are genuinely only partially folded in the transition state. The implications for modeling of protein folding pathways are discussed.},
author_keywords={barnase; chymotrypsin inhibitor 2; linear free-energy relationships},
keywords={chymotrypsin inhibitor, article; barley; enzyme kinetics; genetic engineering; priority journal; protein conformation; protein folding; protein structure, Amino Acid Sequence; Chymotrypsin; Comparative Study; Kinetics; Mathematics; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Plant Proteins; Protein Folding; Protein Structure, Secondary; Recombinant Proteins; Ribonucleases; Support, Non-U.S. Gov't; Thermodynamics, Hordeum vulgare subsp. vulgare},
correspondence_address1={Fersht, A.R.; Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, United Kingdom},
issn={00278424},
coden={PNASA},
pubmed_id={7937968},
language={English},
abbrev_source_title={PROC. NATL. ACAD. SCI. U. S. A.},
document_type={Article},
source={Scopus},
}
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