Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability. (Articolo in rivista)

Type
Label
  • Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/prot.20289 (literal)
Alternative label
  • D'Auria S., Scirè A., Varriale A., Scognamiglio V., Staiano M., Ausili A., Marabotti A., Rossi M., Tanfani F. (2005)
    Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability.
    in Proteins (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • D'Auria S., Scirè A., Varriale A., Scognamiglio V., Staiano M., Ausili A., Marabotti A., Rossi M., Tanfani F. (literal)
Pagina inizio
  • 80 (literal)
Pagina fine
  • 87 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • 6 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 58 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Protein Biochemistry, CNR, Naples, Italy Institute of Biochemistry, Faculty of Sciences, Universita` Politecnica delle Marche, Ancona, Italy Laboratory of Bioinformatics, Institute of Food Science, CNR, Avellino, Italy (literal)
Titolo
  • Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability. (literal)
Abstract
  • Glutamine-binding protein (GlnBP) from Escherichia coli is a monomeric protein localized in the periplasmic space of the bacterium. It is responsible for the first step in the active transport of L-glutamine across the cytoplasmic membrane. The protein consists of two similar globular domains linked by two peptide hinges, and X-ray crystallographic data indicate that the two domains undergo large movements upon ligand binding. Fourier transform infrared spectroscopy (FTIR) was used to analyze the structure and thermal stability of the protein in detail. The data indicate that glutamine binding induces small changes in the secondary structure of the protein and that it renders the structure more thermostable and less flexible. Detailed analyses of IR spectra show a lower thermal sensitivity of alpha-helices than beta-sheets in the protein both in the absence and in the presence of glutamine. Generalized two-dimensional (2D) analyses of IR spectra reveal the same sequence of unfolding events in the protein in the absence and in the presence of glutamine, indicating that the amino acid does not affect the unfolding pathway of the protein. The data give new insight into the structural characteristics of GlnBP that are useful for both basic knowledge and biotechnological applications. (literal)
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