The effect of temperature and glucose binding on the structure of the galactose/glucose-binding protein from Escherichia coli was investigated by circular dichroism, Fourier transform infrared spectroscopy, and steady-state and time-resolved fluorescence. The data showed that the glucose binding induces a moderate change of the secondary structure content of the protein and increases the protein thermal stability. The infrared spectroscopy data showed that some protein stretches, involved in alpha-helices and beta strand conformations, are particularly sensitive to temperature. The fluorescence studies showed that the intrinsic tryptophanyl fluorescence of the protein is well represented by a three-exponential model and that in the presence of glucose the protein adopts a structure less accessible to the solvent. The new insights on the structural properties of the galactose/glucose-binding protein can contribute to a better understanding of the protein functions and represent fundamental information for the development of biotechnological applications of the protein.

Structural and thermal stability characterization of Escherichia coli D-galactose/D-glucose-binding protein / D'Auria, T.; Alfieri, F.; Staiano, M.; Pelella, F.; Rossi, M.; Scire', ANDREA ANTONINO; Tanfani, Fabio; Bertoli, Enrico; Grycznyski, Z.; Lakowicz, R.. - In: BIOTECHNOLOGY PROGRESS. - ISSN 8756-7938. - 20:(2004), pp. 330-337.

Structural and thermal stability characterization of Escherichia coli D-galactose/D-glucose-binding protein

SCIRE', ANDREA ANTONINO;TANFANI, Fabio;BERTOLI, Enrico;
2004-01-01

Abstract

The effect of temperature and glucose binding on the structure of the galactose/glucose-binding protein from Escherichia coli was investigated by circular dichroism, Fourier transform infrared spectroscopy, and steady-state and time-resolved fluorescence. The data showed that the glucose binding induces a moderate change of the secondary structure content of the protein and increases the protein thermal stability. The infrared spectroscopy data showed that some protein stretches, involved in alpha-helices and beta strand conformations, are particularly sensitive to temperature. The fluorescence studies showed that the intrinsic tryptophanyl fluorescence of the protein is well represented by a three-exponential model and that in the presence of glucose the protein adopts a structure less accessible to the solvent. The new insights on the structural properties of the galactose/glucose-binding protein can contribute to a better understanding of the protein functions and represent fundamental information for the development of biotechnological applications of the protein.
2004
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11566/51488
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