The protein dynamical transition does not require the protein polypeptide chain (Articolo in rivista)

Type
Label
  • The protein dynamical transition does not require the protein polypeptide chain (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jz200797g (literal)
Alternative label
  • Giorgio Schir?o,+ Chiara Caronna,? Francesca Natali,§ M. Marek Koza,|| and Antonio Cupane*,+ (2011)
    The protein dynamical transition does not require the protein polypeptide chain
    in The journal of physical chemistry letters
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Giorgio Schir?o,+ Chiara Caronna,? Francesca Natali,§ M. Marek Koza,|| and Antonio Cupane*,+ (literal)
Pagina inizio
  • 2275 (literal)
Pagina fine
  • 2279 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 2 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • +Department of Physics, University of Palermo, Via Archirafi 36, I-90123 Palermo, Italy ?SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States §CNR-IOM, c/o ILL, 6 Rue Jules Horowitz, BP 156-38042 Grenoble, France ll ILL, 6 Rue Jules Horowitz, BP 156-38042 Grenoble, France (literal)
Titolo
  • The protein dynamical transition does not require the protein polypeptide chain (literal)
Abstract
  • We give experimental evidence that the main features of protein dynamics revealed by neutron scattering, i.e., the \"protein dynamical transition\" and the \"boson peak\", do not need the protein polypeptide chain. We show that a rapid increase of hydrogen atoms fluctuations at about 220 K, analogous to the one observed in hydratedmyoglobin powders, is also observed in a hydrated amino acids mixture with the chemical composition of myoglobin but lacking the polypeptide chain; in agreement with the protein behavior, the transition is abolished in the dry mixture. Further, an excess of low-frequency vibrational modes around 3 meV, typically observed in protein powders, is also observed in our mixture. Our results confirm that the dynamical transition is a water-driven onset and indicate that it mainly involves the amino acid side chains. Taking together the present data and recent results on the dynamics of a protein in denatured conformation and on the activity of dehydrated proteins, it can be concluded that the \"protein dynamical transition\" is neither a necessary nor a sufficient condition for active protein conformation and function. (literal)
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