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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: Pressure effect on the stability and the conformational dynamics of the D-Galactose/D-Glucose-binding protein from Escherichia coli.

Anno di pubblicazione: 2006

Autori: Marabotti A., Herman P., Staiano M., Varriale A., de Champdorč M., Rossi M., Gryczynski Z., D'Auria S.

Affiliazioni autori: Laboratory of Bioinformatics, Institute of Food Science, CNR, Avellino, Italy Interdepartmental Research Center for Computational and Biotechnological Sciences (CRISCEB), Second University of Naples,Naples, Italy Faculty of Mathematics and Physics, Institute of Physics, Charles University, Prague, Czech Republic Institute of Protein Biochemistry, CNR, Naples, Italy Center for Fluorescence Spectroscopy, UMAB, Baltimore, Marylan

Autori CNR:

  • SABATO D'AURIA
  • MARCELLA DE CHAMPDORE'
  • ANNA MARABOTTI
  • ANNA MARABOTTI
  • MOSč ROSSI
  • MARIA STAIANO
  • ANTONIO VARRIALE

Abstract: The effect of the pressure on the structure and stability of the D-Galactose/D-Glucose binding protein (GGBP) from Escherichia coli was studied by steady-state and time-resolved fluorescence spectroscopy, and the ability of glucose ligand to stabilize the GGBP structure was also investigated. Steady-state fluorescence experiments showed a marked quenching of fluorescence emission of GGBP in the absence of glucose. Instead, the presence of glucose seems to stabilize the structure of GGBP at low and moderate pressure values. Time-resolved fluorescence measurements showed that the GGBP taumean in the absence of glucose varies significantly up to 600 bar, while in the presence of the ligand it is almost unaffected by pressure increase up to 600 bar. The effect of the pressure on GGBP was also studied by molecular dynamics simulations. The simulation data support the spectroscopic results and confirm that the presence of glucose is able to contrast the negative effects of pressure on the protein structure. Taken together, the spectroscopic and computer simulation studies suggest that at pressure values up to 2000 bar the structure of GGBP in the absence of glucose remains folded, but a significant perturbation of the protein secondary structures can be detected. The binding of glucose reduces the negative effect of pressure on protein structure and confers protection from perturbation especially at moderate pressure values. 2005 Wiley-Liss, Inc.

Pagine da: 193

Pagine a: 201

Rivista:

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

Numero volume: 62

DOI: 10.1002/prot.20753

Altre informazioni: 1

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