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

Andrea Scirè, Anna Marabotti, Vincenzo Aurilia, Maria Staiano, Paola Ringhieri, Luisa Iozzino, Roberta Crescenzo, Fabio Tanfani, Sabato D'Auria

Research output: Contribution to journalArticlepeer-review


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 α-helix conformation with a minor content of β-structure. In this work, we used Fourierinfrared 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 p2H values (neutral p2H and at p 2H 9.8). In the absence of SDS, the results pointed out a high thermostability of the MalE1 α-helices, maintained also at basic p 2H values. However, the obtained data also showed that at high temperatures the MalE1 β-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.

Original languageEnglish
Pages (from-to)839-850
Number of pages12
JournalProteins: Structure, Function and Genetics
Issue number4
Publication statusPublished - Dec 2008


  • FTIR
  • Protein structure
  • Thermus thermophilus
  • Trehalose/maltose-binding protein

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Structural Biology
  • Medicine(all)


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