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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: Wild-type and mutant bovine odorant-binding proteins to probe the role of the quaternary structure organization in the protein thermal stability

Anno di pubblicazione: 2008

Formato: Elettronico

Autori: Marabotti A.; Scirč A.; Staiano M.; Crescenzo R.; Aurilia V.; Tanfani F.; D'Auria S.

Affiliazioni autori: Istituto di Scienze dell'Alimentazione, CNR, Avellino, Italy, Istituto di Biochimica, Universita? Politecnica delle Marche, Ancona, Italy, and Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy

Autori CNR:


Lingua: inglese

Abstract: The exploration of events taking place at different timescales and affecting the structural and dynamics properties of proteins, such as the interactions of proteins with ligands and the subunits association/dissociation, must necessarily be performed by using different methodologies, each of which specialized to highlight the different phenomena that occur when proteins are exposed to chemical or physical stress. In this work, we investigated the structure and dynamics of the wild-type bovine odorant-binding protein (wt-bOBP), which is a domain-swapped dimeric protein, and the triple mutant deswapped monomeric form of the protein (m-bOBP) to shed light on the role of the quaternary and tertiary structural organization in the protein thermal stability. Difference infrared spectra, 2D-IR correlation spectroscopy and molecular dynamics simulations were used to probe the effect of heating on protein structure and dynamics in microsecond and nanoseconds temporal ranges, respectively. The obtained results show that there is a heating-induced transition toward a less structured state in m-bOBP, that it is detectable around 70-80 degrees C. On the contrary, in wt-bOBP this transition is almost negligible, and changes are detectable in the protein spectra in the range of temperature between 75 and 85 degrees C. A detailed 3D inspection of the structure of the two proteins that takes into the account the spectroscopic results indicates that (a) ion pairs and hydrophobic interactions appear to be the major determinants responsible for the protein stability and (b) the protein intersubunit interactions confer an increased resistance toward the thermal stress

Lingua abstract: inglese

Pagine da: 5221

Pagine a: 5229


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

Numero volume: 7

Numero fascicolo: 12

DOI: 10.1021/pr800528b

Referee: Sė: Internazionale

Indicizzato da: ISI Web of Science (WOS) [000261478700017]

Parole chiave:

  • Odorant-binding protein
  • Lipocalins
  • FT-IR
  • MD

Strutture CNR:


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