An obligatory intermediate in the folding pathway of cytochrome c(552) from Hydrogenobacter thermophilus (Articolo in rivista)

Type
Label
  • An obligatory intermediate in the folding pathway of cytochrome c(552) from Hydrogenobacter thermophilus (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M502628200 (literal)
Alternative label
  • Travaglini-Allocatelli, C., Gianni, S., Dubey, V.K., Borgia, A., Di Matteo, A., Bonivento, D., Cutruzzolà, F., Bren, K.L., Brunori, M (2005)
    An obligatory intermediate in the folding pathway of cytochrome c(552) from Hydrogenobacter thermophilus
    in The Journal of biological chemistry (Print); AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, BETHESDA (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Travaglini-Allocatelli, C., Gianni, S., Dubey, V.K., Borgia, A., Di Matteo, A., Bonivento, D., Cutruzzolà, F., Bren, K.L., Brunori, M (literal)
Pagina inizio
  • 25729 (literal)
Pagina fine
  • 25734 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 280 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 27 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Roma La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy CNR, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy Univ Rochester, Dept Chem, Rochester, NY 14627 USA (literal)
Titolo
  • An obligatory intermediate in the folding pathway of cytochrome c(552) from Hydrogenobacter thermophilus (literal)
Abstract
  • The folding mechanism of many proteins involves the population of partially organized structures en route to the native state. Identification and characterization of these intermediates is particularly difficult, as they are often only transiently populated and may play different mechanistic roles, being either on- pathway productive species or off- pathway kinetic traps. Following different spectroscopic probes, and employing state- of- the- art kinetic analysis, we present evidence that the folding mechanism of the thermostable cytochrome c(552) from Hydrogenobacter thermophilus does involve the presence of an elusive, yet compact, on- pathway intermediate. Characterization of the folding mechanism of this cytochrome c is particularly interesting for the purpose of comparative folding studies, because H. thermophilus cytochrome c552 shares high sequence identity and structural homology with its homologue from the mesophilic bacterium Pseudomonas aeruginosa cytochrome c(551), which refolds through a broad energy barrier without the accumulation of intermediates. Analysis of the folding kinetics and correlation with the three- dimensional structure add new evidence for the validity of a consensus folding mechanism in the cytochrome c family. (literal)
Editore
Prodotto di
Autore CNR

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Editore di
data.CNR.it