Resolution of the effects induced by W->F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F (Articolo in rivista)

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  • Resolution of the effects induced by W->F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s00249-012-0829-1 (literal)
Alternative label
  • Infusini G; Iannuzzi C; Vilasi S; Birolo L; Pagnozzi D; Pucci P; Irace G; Sirangelo I (2012)
    Resolution of the effects induced by W->F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F
    in European biophysics journal; Springer, New York (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Infusini G; Iannuzzi C; Vilasi S; Birolo L; Pagnozzi D; Pucci P; Irace G; Sirangelo I (literal)
Pagina inizio
  • 615 (literal)
Pagina fine
  • 627 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://link.springer.com/article/10.1007/s00249-012-0829-1/fulltext.html (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 41 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Biochimica e Biofisica, Seconda Università di Napoli, Via L. De Crecchio 7, 80138 Naples, Italy; Dipartimento di Chimica Organica e Biochimica, Università di Napoli \"Federico II\", Complesso Monte S. Angelo, Naples, Italy; CNR-Istituto di Biofisica, Via U. La Malfa 153, 90146 Palermo, Italy; Istituto Nazionale Biostrutture e Biosistemi, Rome, Italy; MRC-National Institute for Medical Research, London, NW7 1AA, UK (literal)
Titolo
  • Resolution of the effects induced by W->F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F (literal)
Abstract
  • Myoglobin is an alpha-helical globular protein containing two highly conserved tryptophanyl residues at positions 7 and 14 in the N-terminal region. The simultaneous substitution of the two residues increases the susceptibility of the polypeptide chain to misfold, causing amyloid aggregation under physiological condition, i.e., neutral pH and room temperature. The role played by tryptophanyl residues in driving the folding process has been investigated by examining three mutated apomyoglobins, i.e., W7F, W14F, and the amyloid-forming mutant W7FW14F, by an integrated approach based on far-ultraviolet (UV) circular dichroism (CD) analysis, fluorescence spectroscopy, and complementary proteolysis. Particular attention has been devoted to examine the conformational and dynamic properties of the equilibrium intermediate formed at pH 4.0, since it represents the early organized structure from which the native fold originates. The results show that the W -> F substitutions at position 7 and 14 differently affect the structural organization of the AGH subdomain of apomyoglobin. The combined effect of the two substitutions in the double mutant impairs the formation of native-like contacts and favors interchain interactions, leading to protein aggregation and amyloid formation (literal)
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