Dataset Information

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

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.

SUBMITTER: D'Auria S

PROVIDER: S-EPMC6876691 | biostudies-literature | 2004 Jan-Feb

REPOSITORIES: biostudies-literature

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

D'Auria Sabato S Alfieri Fabrizio F Staiano Maria M Pelella Fabrizio F Rossi Mose' M Scirè Andrea A Tanfani Fabio F Bertoli Enrico E Grycznyski Zigmunt Z Lakowicz Joseph R JR

Biotechnology progress 20040101 1

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 alp ...[more]

PMID: 14763860

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Dataset Information

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

Publications

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

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