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

Research output: Contribution to journalArticle

28 Citations (Scopus)

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 - 1 Jan 2004

Fingerprint

Galactose
Carrier Proteins
Hot Temperature
Escherichia coli
Glucose
Fluorescence
Proteins
Secondary Protein Structure
Temperature
Protein Stability
Fourier Transform Infrared Spectroscopy
Circular Dichroism
Spectrum Analysis
galactose-binding protein

Cite this

D'Auria, S., Alfieri, F., Staiano, M., Pelella, F., Rossi, M., Scirè, A., ... 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
D'Auria, Sabato ; Alfieri, Fabrizio ; Staiano, Maria ; Pelella, Fabrizio ; Rossi, Mose' ; Scirè, Andrea ; Tanfani, Fabio ; Bertoli, Enrico ; Grycznyski, Zigmunt ; Lakowicz, Joseph R. / Structural and Thermal Stability Characterization of Escherichia coli D-Galactose/D-Glucose-Binding Protein. In: Biotechnology Progress. 2004 ; Vol. 20, No. 1. pp. 330-337.
@article{637f5106c25343629a1c7fe509983996,
title = "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 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.",
author = "Sabato D'Auria and Fabrizio Alfieri and Maria Staiano and Fabrizio Pelella and Mose' Rossi and Andrea Scir{\`e} and Fabio Tanfani and Enrico Bertoli and Zigmunt Grycznyski and Lakowicz, {Joseph R.}",
year = "2004",
month = "1",
day = "1",
doi = "10.1021/bp0341848",
language = "English",
volume = "20",
pages = "330--337",
journal = "Biotechnology Progress",
issn = "8756-7938",
publisher = "Wiley-Blackwell",
number = "1",

}

D'Auria, S, Alfieri, F, Staiano, M, Pelella, F, Rossi, M, Scirè, A, Tanfani, F, Bertoli, E, Grycznyski, Z & Lakowicz, JR 2004, 'Structural and Thermal Stability Characterization of Escherichia coli D-Galactose/D-Glucose-Binding Protein', Biotechnology Progress, vol. 20, no. 1, pp. 330-337. https://doi.org/10.1021/bp0341848

Structural and Thermal Stability Characterization of Escherichia coli D-Galactose/D-Glucose-Binding Protein. / D'Auria, Sabato; Alfieri, Fabrizio; Staiano, Maria; Pelella, Fabrizio; Rossi, Mose'; Scirè, Andrea; Tanfani, Fabio; Bertoli, Enrico; Grycznyski, Zigmunt; Lakowicz, Joseph R.

In: Biotechnology Progress, Vol. 20, No. 1, 01.01.2004, p. 330-337.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Structural and Thermal Stability Characterization of Escherichia coli D-Galactose/D-Glucose-Binding Protein

AU - D'Auria, Sabato

AU - Alfieri, Fabrizio

AU - Staiano, Maria

AU - Pelella, Fabrizio

AU - Rossi, Mose'

AU - Scirè, Andrea

AU - Tanfani, Fabio

AU - Bertoli, Enrico

AU - Grycznyski, Zigmunt

AU - Lakowicz, Joseph R.

PY - 2004/1/1

Y1 - 2004/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=10744232637&partnerID=8YFLogxK

U2 - 10.1021/bp0341848

DO - 10.1021/bp0341848

M3 - Article

C2 - 14763860

AN - SCOPUS:10744232637

VL - 20

SP - 330

EP - 337

JO - Biotechnology Progress

JF - Biotechnology Progress

SN - 8756-7938

IS - 1

ER -