Thermal Stabilization of Proteins by Mono- and Oligosaccharides: Measurement and Analysis in the Context of an Excluded Volume Model
| Autor: | Faizan Ahmad, Ilyas Beg, Asimul Islam, Allen P. Minton, Imtaiyaz Hassan |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Protein Denaturation Hot Temperature Protein Conformation Oligosaccharides Context (language use) Biochemistry Stachyose Absorbance chemistry.chemical_compound Enzyme Stability Carbohydrate Conformation Animals Raffinose Protein Stability Monosaccharides Osmolar Concentration Fructose Trehalose Molecular Weight Kinetics Crystallography chemistry Excluded volume Lactalbumin Physical chemistry Cattle Muramidase Carbohydrate conformation Apoproteins Chickens |
| Zdroj: | Biochemistry. 54:3594-3603 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/acs.biochem.5b00415 |
| Popis: | The reversible thermal denaturation of apo α-lactalbumin and lysozyme was monitored via measurement of changes in absorbance and ellipticity in the presence of varying concentrations of seven mono- and oligosaccharides: glucose, galactose, fructose, sucrose, trehalose, raffinose, and stachyose. The temperature dependence of the unfolding curves was quantitatively accounted for by a two-state model, according to which the free energy of unfolding is increased by an amount that is independent of temperature and depends linearly upon the concentration of added saccharide. The increment of added unfolding free energy per mole of added saccharide was found to depend approximately linearly upon the extent of oligomerization of the saccharide. The relative strength of stabilization of different saccharide oligomers could be accounted for by a simplified statistical-thermodynamic model attributing the stabilization effect to volume exclusion deriving from steric repulsion between protein and saccharide molecules. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|