An on-pathway intermediate in the folding of a PDZ domain. (Articolo in rivista)

Type
Label
  • An on-pathway intermediate in the folding of a PDZ domain. (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Alternative label
  • Ivarsson Y, Travaglini-Allocatelli C, Jemth P, Malatesta F, Brunori M, Gianni S. (2007)
    An on-pathway intermediate in the folding of a PDZ domain.
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ivarsson Y, Travaglini-Allocatelli C, Jemth P, Malatesta F, Brunori M, Gianni S. (literal)
Pagina inizio
  • 8568 (literal)
Pagina fine
  • 8572 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 282 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche \"A. Rossi Fanelli,\" Universita` di Roma\"La Sapienza,\" Piazzale A. Moro 5, 00185 Rome, Italy, the Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-75123 Uppsala, Sweden, and the Department of Pure and Applied Biology, University of L'Aquila, 67010 L'Aquila, Italy (literal)
Titolo
  • An on-pathway intermediate in the folding of a PDZ domain. (literal)
Abstract
  • The folding pathways of some proteins include the population of partially structured species en route to the native state. Identification and characterization of these folding intermediates are particularly difficult as they are often only transiently populated and play different mechanistic roles, being either on-pathway productive species or off-pathway kinetic traps. To define the role of folding intermediates, a quantitative analysis of the folding and unfolding rate constants over a wide range of denaturant concentration is often required. Such a task is further complicated by the reversible nature of the folding reaction, which implies the observed kinetics to be governed by a complex combination of different microscopic rate constants. Here, we tackled this problem by measuring directly the folding rate constant under highly denaturing conditions, namely by inducing the folding of a PDZ domain through a quasi-irreversible binding reaction with a specific peptide. In analogy with previous works based on hydrogen exchange experiments, we present evidence that the folding pathway of the PDZ domain involves the formation of an obligatory on-pathway intermediate. The results presented exemplify a novel type of kinetic test to detect an on-pathway folding intermediate. (literal)
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