Title
The pH Dependence of Saccharides’ Influence on Thermal Denaturation of Two Model Proteins Supports an Excluded Volume Model for Stabilization Generalized to Allow for Intramolecular Electrostatic Interactions
Author
Ilyas Beg, Allen P. Minton, Asimul Islam, Md. Imtaiyaz Hassan, Faizan Ahmad
Year
2016
Journal
The Journal of Biological Chemistry
Abstract
The reversible thermal denaturation of apo α-lactalbumin (α-LA) and lysozyme was measured in the absence and presence of multiple concentrations of each of seven saccharides (glucose, galactose, fructose, sucrose, trehalose, raffinose, and stachyose) at multiple pH values. It was observed that with increasing pH, the absolute stability of α-LA decreased, whereas the stabilizing effect per mole of all saccharides increased, and that the absolute stability of lysozyme increased, whereas the stabilizing effect per mole of all saccharides decreased. All of the data may be accounted for quantitatively by straightforward electrostatic generalization of a previously introduced coarse-grained model for stabilization of proteins by sugars.
Full Article
Instrument
J-1500
Keywords
Circular dichroism, Secondary structure, Chemical stability, Protein denaturation, Thermal stability, Thermodynamics, Biochemistry