Calorimetric study of myoglobin embedded in trehalose-water matrixes

It has been suggested that in ‘dry’ protein-trehalose-water systems, water-mediated hydrogen bond network, whose strength increases by drying, anchors the protein to its surroundings. To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denatura...

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Veröffentlicht in:Journal of thermal analysis and calorimetry 2009-03, Vol.95 (3), p.699-702
Hauptverfasser: Bellavia, G., Cordone, L., Cupane, A.
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Cordone, L.
Cupane, A.
description It has been suggested that in ‘dry’ protein-trehalose-water systems, water-mediated hydrogen bond network, whose strength increases by drying, anchors the protein to its surroundings. To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denaturation temperature resulted to increase by decreasing hydration, and linearly correlated to the glass transition temperature of both the ternary protein-water-trehalose and the binary water-trehalose systems. Further measurements are being performed to investigate eventual differences among different saccharides.
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subjects Analytical Chemistry
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Biological Materials
Chemistry
Chemistry and Materials Science
Fundamental and applied biological sciences. Psychology
Hemoproteins
Inorganic Chemistry
Measurement Science and Instrumentation
Metalloproteins
Physical Chemistry
Polymer Sciences
Proteins
title Calorimetric study of myoglobin embedded in trehalose-water matrixes
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