ArticleBiotechnology progress
Structural and thermal stability characterization of Escherichia coli D-galactose/D-glucose-binding protein.
Article in Biotechnology progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 26 citations in OpenAlex.
- A modified fluorescent sensor for reporting glucose concentration in the airway lumen.PloS one · 2021Article
- Tryptophan residue of the D-galactose/D-glucose-binding protein from E. Coli localized in its active center does not contribute to the change in intrinsic fluorescence upon glucose binding.Journal of fluorescence · 2015Article
- Computational design of ligand binding is not a solved problem.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- D-galactose/D-glucose-binding Protein from Escherichia coli as Probe for a Non-consuming Glucose Implantable Fluorescence Biosensor.Sensors (Basel, Switzerland) · 2007Article
- Protein free energy landscapes remodeled by ligand binding.Biophysical journal · 2007Article
- Fluorescence glucose detection: advances toward the ideal in vivo biosensor.Journal of fluorescence · 2004Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
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.
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Registered trials
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