PMID:14763860

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Citation

D'Auria, S, Alfieri, F, Staiano, M, Pelella, F, Rossi, M, Scirè, A, Tanfani, F, Bertoli, E, Grycznyski, Z and Lakowicz, JR Structural and thermal stability characterization of Escherichia coli D-galactose/D-glucose-binding protein. Biotechnol. Prog. 20:330-7

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.

Links

PubMed Online version:10.1021/bp0341848

Keywords

Computer Simulation; Escherichia coli/metabolism; Escherichia coli Proteins/analysis; Escherichia coli Proteins/chemistry; Models, Molecular; Monosaccharide Transport Proteins/analysis; Monosaccharide Transport Proteins/chemistry; Protein Conformation; Protein Structure, Secondary; Temperature

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