Structural and Thermal Stability Characterization of Escherichia coli D-Galactose/D-Glucose-Binding Protein

Sabato D'Auria, Fabrizio Alfieri, Maria Staiano, Fabrizio Pelella, Mose' Rossi, Andrea Scirè, Fabio Tanfani, Enrico Bertoli, Zigmunt Grycznyski, Joseph R. Lakowicz

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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 α-helices and β 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.

Original languageEnglish
Pages (from-to)330-337
Number of pages8
JournalBiotechnology Progress
Volume20
Issue number1
DOIs
StatePublished - Jan 2004

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    D'Auria, S., Alfieri, F., Staiano, M., Pelella, F., Rossi, M., Scirè, A., Tanfani, F., Bertoli, E., Grycznyski, Z., & Lakowicz, J. R. (2004). Structural and Thermal Stability Characterization of Escherichia coli D-Galactose/D-Glucose-Binding Protein. Biotechnology Progress, 20(1), 330-337. https://doi.org/10.1021/bp0341848