Home |  English version |  Mappa |  Commenti |  Sondaggio |  Staff |  Contattaci Cerca nel sito  
Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2008

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Molecular strategies for protein stabilization: the case of a trehalose/maltose-binding protein from Thermus thermophilus.

Anno di pubblicazione: 2008

Formato: Elettronico

Autori: Scirč A, Marabotti A, Aurilia V, Staiano M, Ringhieri P, Iozzino L, Crescenzo R, Tanfani F, D'Auria S.

Affiliazioni autori: Institute of Biochemistry, Faculty of Sciences, Universita Politecnica delle Marche, Ancona, Italy Institute of Food Science, CNR, Avellino, Italy Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy

Autori CNR:

  • VINCENZO AURILIA
  • ROBERTA CRESCENZO
  • SABATO D'AURIA
  • LUISA IOZZINO
  • ANNA MARABOTTI
  • ANNA MARABOTTI
  • MARIA STAIANO

Lingua: inglese

Abstract: The trehalose/maltose-binding protein (MalE1) is one component of trehalose and maltose uptake system in the thermophilic organism Thermus thermophilus. MalE1 is a monomeric 48 kDa protein predominantly organized in alpha-helix conformation with a minor content of beta-structure. In this work, we used Fourier-infrared spectroscopy and in silico methodologies for investigating the structural stability properties of MalE1. The protein was studied in the absence and in the presence of maltose as well as in the absence and in the presence of SDS at different p(2)H values (neutral p(2)H and at p(2)H 9.8). In the absence of SDS, the results pointed out a high thermostability of the MalE1 alpha-helices, maintained also at basic p(2)H values. However, the obtained data also showed that at high temperatures the MalE1 beta-sheets underwent to structural rearrangements that were totally reversible when the temperature was lowered. At room temperature, the addition of SDS to the protein solution slightly modified the MalE1 secondary structure content by decreasing the protein thermostability. The infrared data, corroborated by molecular dynamics simulation experiments performed on the structure of MalE1, indicated that the protein hydrophobic interactions have an important role in the MalE1 high thermostability. Finally, the results obtained on MalE1 are also discussed in comparison with the data on similar thermostable proteins already studied in our laboratories.

Pagine da: 839

Pagine a: 850

Rivista:

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

Numero volume: 73

Referee: Sė: Internazionale

Strutture CNR:

Moduli:

 
Torna indietro Richiedi modifiche Invia per email Stampa
Home Il CNR  |  I servizi News |   Eventi | Istituti |  Focus