The influence of macromolecular crowding on HIV-1 protease internal dynamics (Articolo in rivista)

Type
Label
  • The influence of macromolecular crowding on HIV-1 protease internal dynamics (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/ja060483s (literal)
Alternative label
  • Minh, DDL; Chang, CE; Trylska, J; Tozzini, V; McCammon, JA (2006)
    The influence of macromolecular crowding on HIV-1 protease internal dynamics
    in Journal of the American Chemical Society (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Minh, DDL; Chang, CE; Trylska, J; Tozzini, V; McCammon, JA (literal)
Pagina inizio
  • 6006 (literal)
Pagina fine
  • 6007 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 128 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Calif San Diego, Ctr Theoret Biol Phys, Dept Chem & Biochem, San Diego, CA 92093 USA; Univ Calif San Diego, Howard Hughes Med Inst, Dept Pharmacol, San Diego, CA 92093 USA; Warsaw Univ, Interdisciplinary Ctr Math & Computat Modelling, PL-02106 Warsaw, Poland; Scuola Normale Super Pisa, NEST, I-56126 Pisa, Italy (literal)
Titolo
  • The influence of macromolecular crowding on HIV-1 protease internal dynamics (literal)
Abstract
  • High macromolecular concentrations, or crowded conditions, have been shown to affect a wide variety of molecular processes, including diffusion, association and dissociation, and protein folding and stability. Here, we model the effect of macromolecular crowding on the internal dynamics of a protein, HIV-1 protease, using Brownian dynamics simulations. HIV-1 protease possesses a pair of flaps which are postulated to open in the early stages of its catalytic mechanism. Compared to low concentrations, close-packed concentrations of repulsive crowding agents are found to significantly reduce the fraction of time that the protease flaps are open. Macromolecular crowding is likely to have a major effect on in vivo enzyme activity, and may play an important regulatory role in the viral life cycle. (literal)
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