Engineered symmetric connectivity highlights malleability in protein folding pathways (Articolo in rivista)

Type
Label
  • Engineered symmetric connectivity highlights malleability in protein folding pathways (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Alternative label
  • Ivarsson, Y., Travaglini-Allocatelli, C., Brunori, M., Gianni, S. (2009)
    Engineered symmetric connectivity highlights malleability in protein folding pathways
    in Journal of the American Chemical Society (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ivarsson, Y., Travaglini-Allocatelli, C., Brunori, M., Gianni, S. (literal)
Pagina inizio
  • 11727 (literal)
Pagina fine
  • 11733 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 131 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto Pasteur - Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche \"A. Rossi Fanelli\", UniVersita` di Roma \"La Sapienza\", Piazzale A. Moro 5, 00185 Rome, Italy (literal)
Titolo
  • Engineered symmetric connectivity highlights malleability in protein folding pathways (literal)
Abstract
  • To understand the role of sequence connectivity in protein folding pathways, we explored by Phi-value analysis the folding pathway of an engineered circularly permuted PDZ domain. This variant has the same sequence connectivity as naturally occurring circularly permuted PDZ domains and displays a symmetrical distribution of secondary structure elements (i.e., beta beta alpha beta beta alpha beta beta) while maintaining the same tertiary interactions of the well-characterized second PDZ domain from PTP-BL (PDZ2). Reliable Phi values were obtained for both a low-energy intermediate and the late rate-limiting transition state, allowing a description of both early and late events in folding. A comparison with Phi values obtained for wild-type PDZ2 reveals that while the structure of the late transition state is robust and unaffected by circular permutation, the folding intermediate is stabilized by a different nucleus involving residues located at the new N- and C-termini. The results suggest that folding is driven by competing nuclei whose stabilities may be selectively tuned by circular permutation. (literal)
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