Chemical denaturation and thermal denaturation of13-lactoglobulin A (f3 — lgA) in the absenceand presence of various concentrations sugar osmolytes and polyols were measured bymonitoring changes in the absorption coefficients at pH 2.0. It has been observed that AGD°(H20), (Gibbs free energy change in absence of denaturant at 25 °C) of f3-1gA in the presenceof 10% (w/v) Trehalose, Sucrose, Sorb...

Thermal denaturation of a-Lactalbumin in the absence and presence of various concentrations of sucrose,sorbitol, glucose and galactose as sugar osmolytes were measured by monitoring changes in the absorptions thatcarried out in a Lambd 35 UV-Vis double beam spectrophotometer at pH 6.0. These measurements gave valuesof T., (midpoint of denaturation), AH., (enthalpy change at T.), and ACp (consta...

We study the solvation of amino acids in pure-osmolyte and mixed-osmolyte urea and trimethylamine N-oxide (TMAO) solutions using molecular dynamics simulations. Analysis of Kirkwood-Buff integrals between the solution components provides evidence that in the mixed osmolytic solution, both urea and TMAO are mutually excluded from the amino acid surface, accompanied by an increase in osmolyte-osm...

We systematically investigated effects of molecular crowding with trimethylamine N-oxide (TMAO) as a zwitterionic and protective osmolyte and urea as a nonionic denaturing osmolyte on conformation and thermodynamics of the canonical DNA duplex and the non-canonical DNA G-quadruplex. It was found that TMAO and urea stabilized and destabilized, respectively, the G-quadruplex. On the other hand, t...

We seek to understand the link between protein thermodynamics and protein structure in molecular detail. A classical approach to this problem involves assessing changes in protein stability resulting from added cosolvents. Under any given conditions, protein molecules in aqueous buffer are in equilibrium between unfolded and folded states, U(nfolded) <==> N(ative). Addition of organic osmolytes...

Osmolytes are small organic compounds that confer to the cell an enhanced adaptability to external conditions. Many osmolytes not only protect the cell from osmotic stress but also stabilize the native structure of proteins. While simplified models able to predict changes to protein stability are available, a general physicochemical explanation of the underlying microscopic mechanism is still m...

Cellular methylamines are osmolytes (low molecular weight organic compounds) believed to offset the urea's harmful effects on the stability and function of proteins in mammalian kidney and marine invertebrates. Although urea and methylamines are found at 2:1 molar ratio in tissues, their opposing effects on protein structure and function have been questioned on several grounds including failure...

The halophilic methanogen Methanohalophilus portucalensis synthesizes three distinct zwitterions, (beta)-glutamine, N(sup(epsilon))-acetyl-(beta)-lysine (NA(beta)Lys), and glycine betaine, as osmolytes when it is grown at high concentrations of external NaCl. The selective distribution of these three species was determined by growing cells in the presence of osmolyte biosynthetic precursors. Gl...

Protein misfolding and aggregation are responsible for a large number of diseases called protein conformational diseases or disorders that include Alzheimer׳s disease, Huntington׳s diseases, Prion related encephalopathies and type-II diabetes (http://dx.doi.org/10.1038/35041139) (Kopito and Ron, 2000) [1]. A variety of studies have shown that some small organic molecules, known as osmolytes hav...