lithium-chloride and sodium-sulfate

lithium-chloride has been researched along with sodium-sulfate* in 2 studies

Other Studies

2 other study(ies) available for lithium-chloride and sodium-sulfate

Article	Year
Effect of Hofmeister Ions on Transport Properties of Aqueous Solutions of Sodium Hyaluronate. International journal of molecular sciences, 2021, Feb-16, Volume: 22, Issue:4 Tracer diffusion coefficients obtained from the Taylor dispersion technique at 25.0 °C were measured to study the influence of sodium, ammonium and magnesium salts at 0.01 and 0.1 mol dm Topics: Ammonium Sulfate; Anions; Biological Transport; Cations; Diffusion; Hyaluronic Acid; Lithium Chloride; Magnesium Sulfate; Osmolar Concentration; Salts; Sodium Chloride; Solutions; Sulfates; Temperature; Thiocyanates; Viscosity; Water	2021
Hofmeister effects in protein unfolding kinetics: estimation of changes in surface area upon formation of the transition state. Biochimica et biophysica acta, 2006, Volume: 1764, Issue:7 We studied the effect of three electrolytes (LiCl, Na(2)SO(4), GuHCl) on the unfolding reaction of chymopapain, a two-domain protein belonging in the papain family of cysteine proteinases. Due to methodological reasons, these studies were carried out at pH 1.5 where the protein unfolds following biphasic kinetics. We have observed the presence of two different effects of electrolyte concentration on the unfolding reactions. At low ionic strength, the ionic atmosphere brought about an increase in reaction rates, regardless of the type of ions being present; this effect is attributed to a general "electrostatic screening" of charge-charge interactions in the macromolecule. At high ionic strength, each electrolyte exerted a distinctively different effect: both rate constants were largely increased by GuHCl (a well-known protein denaturant), but only slightly by LiCl; in contrast, Na(2)SO(4) (a good precipitant) decreased the value of both unfolding rates. These ion-specific (Hofmeister) effects were further used to estimate changes in accessible surface area (DeltaASA) upon formation of the transition states (TS) for unfolding. Results obtained with LiCl and Na(2)SO(4), which we analyzed by means of a parameterization derived from published solubility data of amino acid derivatives, are consistent with DeltaASA increments (for each phase) of about 8.0% of the total theoretical DeltaASA for complete unfolding of the chymopapain molecule. Results in the presence of GuHCl, which were analyzed by using a previous parameterization of protein unfolding data, gave larger DeltaASAs of activation, equivalent to 13 and 16% of the total unfolding DeltaASA. Topics: Chymopapain; Circular Dichroism; Guanidine; Hydrogen-Ion Concentration; Kinetics; Lithium Chloride; Osmolar Concentration; Protein Conformation; Protein Folding; Static Electricity; Sulfates; Thermodynamics	2006

Article

Year

Effect of Hofmeister Ions on Transport Properties of Aqueous Solutions of Sodium Hyaluronate.

International journal of molecular sciences, 2021, Feb-16, Volume: 22, Issue:4

Tracer diffusion coefficients obtained from the Taylor dispersion technique at 25.0 °C were measured to study the influence of sodium, ammonium and magnesium salts at 0.01 and 0.1 mol dm

Topics: Ammonium Sulfate; Anions; Biological Transport; Cations; Diffusion; Hyaluronic Acid; Lithium Chloride; Magnesium Sulfate; Osmolar Concentration; Salts; Sodium Chloride; Solutions; Sulfates; Temperature; Thiocyanates; Viscosity; Water

2021

Hofmeister effects in protein unfolding kinetics: estimation of changes in surface area upon formation of the transition state.

Biochimica et biophysica acta, 2006, Volume: 1764, Issue:7

We studied the effect of three electrolytes (LiCl, Na(2)SO(4), GuHCl) on the unfolding reaction of chymopapain, a two-domain protein belonging in the papain family of cysteine proteinases. Due to methodological reasons, these studies were carried out at pH 1.5 where the protein unfolds following biphasic kinetics. We have observed the presence of two different effects of electrolyte concentration on the unfolding reactions. At low ionic strength, the ionic atmosphere brought about an increase in reaction rates, regardless of the type of ions being present; this effect is attributed to a general "electrostatic screening" of charge-charge interactions in the macromolecule. At high ionic strength, each electrolyte exerted a distinctively different effect: both rate constants were largely increased by GuHCl (a well-known protein denaturant), but only slightly by LiCl; in contrast, Na(2)SO(4) (a good precipitant) decreased the value of both unfolding rates. These ion-specific (Hofmeister) effects were further used to estimate changes in accessible surface area (DeltaASA) upon formation of the transition states (TS) for unfolding. Results obtained with LiCl and Na(2)SO(4), which we analyzed by means of a parameterization derived from published solubility data of amino acid derivatives, are consistent with DeltaASA increments (for each phase) of about 8.0% of the total theoretical DeltaASA for complete unfolding of the chymopapain molecule. Results in the presence of GuHCl, which were analyzed by using a previous parameterization of protein unfolding data, gave larger DeltaASAs of activation, equivalent to 13 and 16% of the total unfolding DeltaASA.

Topics: Chymopapain; Circular Dichroism; Guanidine; Hydrogen-Ion Concentration; Kinetics; Lithium Chloride; Osmolar Concentration; Protein Conformation; Protein Folding; Static Electricity; Sulfates; Thermodynamics

2006