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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: Mutant bovine odorant-binding protein: temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations.

Anno di pubblicazione: 2008

Autori: Marabotti A, Lefevre T, Staiano M, Crescenzo R, Varriale A, Rossi M, Pezolet M, D'Auria S.

Affiliazioni autori: Istituto di Scienze dell'Alimentazione, CNR, Avellino, Italy CERSIM/CREFSIP, DeŽpartement de Chimie, UniversiteŽLaval, QueŽbec, QueŽbec, Canada Istituto di Biochimica delle Proteine, CNR,Naples, Italy

Autori CNR:

  • ROBERTA CRESCENZO
  • SABATO D'AURIA
  • ANNA MARABOTTI
  • ANNA MARABOTTI
  • MOSè ROSSI
  • MARIA STAIANO
  • ANTONIO VARRIALE

Abstract: Bovine odorant-binding protein (bOBP), a member of the lipocalin family, presents the so-called 3D "domain-swapped" protein structure. In fact, in solution, it appears as a dimer in which each monomer is composed by the classical lipocalin fold, with a central beta-barrel followed by a stretch of residues and the alpha-helix domain protruding out of the barrel and crossing the dimer interface. Recently, a deswapped mutant form of bOBP was obtained, in which a Gly residue was inserted after position 121 and the two residues in position 64 and 156 were replaced by Cys residues for restoring the disulfide bridge common to the lipocalin family. In this work, we used Fourier transform infrared spectroscopy and molecular dynamics simulations to investigate the effect of temperature on the structural stability and conformational dynamics of the mutant bOBP. The spectroscopic and molecular simulation data pointed out that the hydrophobic regions of the protein matrix appear to be an important factor for the protein stability and integrity. In addition, it was also found that the mutant bOBP is significantly stabilized by the binding of the ligand, which may have an impact on the biological function of bOBP. The obtained results will allow for a better use of this protein as probe for the design of advanced protein-based biosensors for the detection of compounds used in the fabrication of explosive powders. (c) 2008 Wiley-Liss, Inc.

Pagine da: 769

Pagine a: 778

Rivista:

Proteins John Wiley & Sons
Paese di pubblicazione: Stati Uniti d'America
Lingua: inglese
ISSN: 1097-0134

Numero volume: 72(2)

DOI: 10.1002/prot.21966

Strutture CNR:

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