Influence of morphological and conformational changes on the molecular mobility in poly(ethylene naphthalene-2,6-dicarboxylate)

2004 ◽  
Vol 212 (1) ◽  
pp. 479-484 ◽  
Author(s):  
Didier Colombini ◽  
Noureddine Zouzou ◽  
Juan Jorge Martinez-Vega
Keyword(s):  
Conformational Changes ◽  
Molecular Mobility ◽  
Poly Ethylene

Molecular Mobility in Amorphous Biobased Poly(ethylene 2,5-furandicarboxylate) and Poly(ethylene 2,4-furandicarboxylate)

2018 ◽  
Vol 51 (5) ◽  
pp. 1937-1945 ◽  
Author(s):  
Aurélie Bourdet ◽  
Antonella Esposito ◽  
Shanmugam Thiyagarajan ◽  
Laurent Delbreilh ◽  
Frédéric Affouard ◽  
...  
Keyword(s):  
Molecular Mobility ◽  
Poly Ethylene

scholarly journals Binding of sorbitol 6-phosphate and of fructose 1-phosphate to the regulatory protein of liver glucokinase

1992 ◽  
Vol 286 (1) ◽  
pp. 253-256 ◽  
Author(s):  
A Vandercammen ◽  
M Detheux ◽  
E Van Schaftingen
Keyword(s):  
Ethylene Glycol ◽  
Conformational Changes ◽  
Binding Assay ◽  
Regulatory Protein ◽  
Free Ligand ◽  
Phosphate Esters ◽  
Poly Ethylene Glycol ◽  
Apparent Affinity ◽  
Poly Ethylene ◽  
Scatchard Plots

Using a binding assay in which the ligand-protein complex is separated from free ligand by precipitation with poly(ethylene glycol) 6000, we found that the regulatory protein of rat liver glucokinase bound close to 1 mol of radiolabelled sorbitol 6-phosphate, a negative effector, or of fructose 1-phosphate, a positive effector, per mol of regulatory protein. Scatchard plots were linear, the dissociation constant being 0.3 microM for both phosphate esters. Sorbitol 6-phosphate and fructose 1-phosphate competed with each other for the binding. Competition was also observed with psicose 1-phosphate, ribitol 5-phosphate, arabitol 5-phosphate and 3-phosphoglycerate, all of which are known to affect the inhibition exerted by the regulatory protein. At a concentration of 10%, poly(ethylene glycol) 6000 decreased the concentration of regulatory protein causing 50% inhibition to a larger extent in the absence (12-fold) than in the presence (3-fold) of a saturating concentration of fructose 6-phosphate, another negative effector. Furthermore, it increased by about 3-fold the apparent affinity for inhibitory phosphate esters, indicating that it induced conformational changes of the regulatory protein.

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