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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2006

Contributo in rivista

Tipo: Articolo in rivista

Titolo: D-Trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis: the binding of trehalose and maltose results in different protein conformational states.

Anno di pubblicazione: 2006

Autori: Herman P., Staiano M., Marabotti A., Varriale A., Scire A., Tanfani F., Vecer J., Rossi M., D'Auria S.

Affiliazioni autori: Faculty of Mathematics and Physics, Institute of Physics, Charles University, Prague, Czech Republic Institute of Protein Biochemistry, CNR, Naples, Italy Laboratory of Bioinformatics, Institute of Food Science, CNR, Avellino, Italy Interdepartmental Research Center for Computational and Biotechnological Sciences, Second University of Naples,Napoli, Institute of Biochemistry, Polytechnical University of Marche, Ancona, Italy

Autori CNR:

  • SABATO D'AURIA
  • ANNA MARABOTTI
  • ANNA MARABOTTI
  • MOSŤ ROSSI
  • MARIA STAIANO
  • ANTONIO VARRIALE

Abstract: In this work, we used fluorescence spectroscopy, molecular dynamics simulation, and Fourier transform infrared spectroscopy for investigating the effect of trehalose binding and maltose binding on the structural properties and the physical parameters of the recombinant D-trehalose/D-maltose binding protein (TMBP) from the hyperthermophilic archaeon Thermococcus litoralis. The binding of the two sugars to TMBP was studied in the temperature range 20 degrees-100 degrees C. The results show that TMBP possesses remarkable temperature stability and its secondary structure does not melt up to 90 degrees C. Although both the secondary structure itself and the sequence of melting events were not significantly affected by the sugar binding, the protein assumes different conformations with different physical properties depending whether maltose or trehalose is bound to the protein. At low and moderate temperatures, TMBP possesses a structure that is highly compact both in the absence and in the presence of two sugars. At about 90 degrees C, the structure of the unliganded TMBP partially relaxes whereas both the TMBP/maltose and the TMBP/trehalose complexes remain in the compact state. In addition, Fourier transform infrared results show that the population of alpha-helices exposed to the solvent was smaller in the absence than in the presence of the two sugars. The spectroscopic results are supported by molecular dynamics simulations. Our data on dynamics and stability of TMBP can contribute to a better understanding of transport-related functions of TMBP and constitute ground for targeted modifications of this protein for potential biotechnological applications. 2006 Wiley-Liss, Inc.

Pagine da: 754

Pagine a: 767

Rivista:

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

Numero volume: 63

DOI: 10.1002/prot.20952

Altre informazioni: 7

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