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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2008

Contributo in rivista

Tipo: Articolo in rivista

Titolo: The tryptophan phosphorescence of porcine and mutant bovine odorant-binding proteins: a probe for the local protein structure and dynamics

Anno di pubblicazione: 2008

Formato: Elettronico

Autori: D'Auria S.; Staiano M.; Varriale A.; Gonnelli M.; Marabotti A.; Rossi M.; Strambini GB.

Affiliazioni autori: Istituto di Biochimica delle Proteine, CNR, Via Pietro Castellino, 111 80131 Naples, Italy, Istituto di Biofisica, CNR Via Moruzzi 1, 56124 Pisa, Italy, and Istituto di Scienze dell'Alimentazione, CNR, Avellino, Italy

Autori CNR:


Lingua: inglese

Abstract: Vertebrate odorant-binding proteins (OBPs) are small extracellular proteins belonging to the lipocalin superfamily. They have been supposed to play a role in events of odorant molecules detection by carrying, deactivating, and/or selecting odorant molecules. The OBPs share a conserved folding pattern, an eight-stranded beta-barrel flanked by an alpha-helix at the C-terminal end of the polypeptide chain. The beta-barrel creates a central nonpolar cavity whose role is to bind and transport hydrophobic odorant molecules. These proteins reversibly bind odorant molecules with dissociation constants ranging from nanomolar to micromolar range. In this work, we have studied the structural features of the OBP from pig and from cow by phosphorescence spectroscopy. The obtained results demonstrate that the indolic phosphorescence of the two studied proteins can be readily detected at ambient temperature solutions and that it is owed exclusively to the internal tryptophan residue located next to the ligand binding cavity, which is generally conserved in the mammalian OBPs. In addition, while both the phosphorescence spectrum and the lifetime yield a picture of the fold of the studied protein in good agreement with the protein crystallographic structures, the triplet probe points out that in solution the polypeptide structure of the both investigated OBPs exists as a multiplicity of slowly interconverting protein conformations. Finally, this work also demonstrates that it is possible to directly detect the binding of the ligands to OBPs as variations of the protein luminescence features, thus, representing the very first observation reported in the literature so far that a fast and direct assay can be used for monitoring the binding of ligands to OBPs.

Lingua abstract: inglese

Pagine da: 1151

Pagine a: 1158


Journal of proteome research American Chemical Society,
Paese di pubblicazione: Stati Uniti d'America
Lingua: inglese
ISSN: 1535-3893

Numero volume: 7

Numero fascicolo: 3

DOI: 10.1021/pr700755z

Referee: Sė: Internazionale

Indicizzato da: ISI Web of Science (WOS) [000253825100030]

Parole chiave:

  • phosphorescence spectroscopy
  • protein dynamics
  • protein conformation
  • biosensors
  • time-resolved luminescence

Strutture CNR:


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