[Stability of sugar-binding proteins: D-galactose/D-glucose-binding protein from Escherichia coli and trehalose/maltose-binding protein from Thermococcus litoralis].
In this work we studied the structure and stability of sugar-binding proteins from mesophilic and thermophilic organisms which are of great importance for their possible use as sensing probe of biosensors aimed to glucose detection in the blood. The data obtained revealed the stabilizing effect of ligands on the structures of D-galactose/D-glucose-binding protein (GGBP) from Escherichia coli and trehalose/maltose-binding protein from thermophilic bacterium Thermococcus litoralis. It was found that TMBP possess an increased stability as its structure remains native even under heating up to 95 degrees C.
Ol'ga V
OV
Stepanenko
O I
OI
Povarova
A V
AV
Fonin
Olesia V
OV
Stepanenko
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D006358:Hot Temperature; D058619:Maltose-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D009004:Monosaccharide Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D055550:Protein Stability; D019712:Thermococcus / Q000737:chemistry* / Q000378:metabolism
D019843:Archaeal Proteins; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; C509064:mglB protein, E coli