potassium-fluoride has been researched along with cesium-chloride* in 2 studies
2 other study(ies) available for potassium-fluoride and cesium-chloride
| Article | Year |
|---|---|
Structure-thermodynamics relation of electrolyte solutions.
The structure of aqueous LiCl, NaCl, KCl, CsCl, KF, and NaI solutions is calculated by molecular dynamics (MD) simulations of the frequently employed Dang force-field in SPC/E water. By using liquid state theory, we integrate the structure to obtain the electrolytes' osmotic coefficient phi and systematically investigate force-field quality and structural consequences to ion-specific bulk thermodynamics. The osmotic coefficients phi(chi) calculated from the exact compressibility route for the cation-Cl(-) force-fields match experiments for concentrations rho approximately < 2M, while NaI and KF parameters fail. Comparison of phi(chi) with phi(v) from the virial route, which relies on the pair potential approximation, shows that many-body effects become important for all salts above rho approximately 0.5M. They can be efficiently corrected, however, by employing a salt-type and rho-dependent dielectric constant epsilon(rho), generalizing previous observations on NaCl only. For physiological concentrations, rho approximately < 0.5M, the specific osmotic behavior is found to be determined by the short-ranged cation-anion pair potential only and is strongly related to the second virial coefficient of the latter. Presented methods and findings, based on simple integrations over the electrolyte structure, enable efficient MD force-field refinement by direct benchmarking to the sensitive electrolyte thermodynamics, instead to noncollective, single ion properties. Topics: Cesium; Chlorides; Electrolytes; Fluorides; Lithium Chloride; Potassium Chloride; Potassium Compounds; Sodium Chloride; Sodium Iodide; Solutions; Thermodynamics | 2009 |
Common components of patch-clamp internal recording solutions can significantly affect protein kinase A activity.
Common components of whole-cell internal recording solutions were tested both in vitro and in patch-clamp experiments for their effects on the activity of cAMP-dependent protein kinase. Potassium fluoride (KF), 440 mM trimethylamine chloride and exclusion of bovine serum albumin (BSA) decreased the activity of the enzyme, while ethylene glycol-bis (beta-aminoethyl ether) N,N,N',N'-tetraacetic acid (EGTA) and the potassium salts of aspartate, gluconate, methylsulfate and monobasic phosphate increased its activity. Addition of KF to the internal solution produced a hyperpolarizing shift in the V1/2 of Ih channel activation, consistent with the KF-induced reduction of protein kinase A activity. Therefore, consideration of the composition of internal solutions is warranted when studying channel physiology by patch-clamp techniques. Topics: Animals; Aspartic Acid; Calcium; Cells, Cultured; Cesium; Chelating Agents; Chlorides; Cyclic AMP-Dependent Protein Kinases; Egtazic Acid; Enzyme Activation; Enzyme Inhibitors; Fluorides; Gluconates; Ion Channels; Isoquinolines; Methylamines; Olfactory Receptor Neurons; Patch-Clamp Techniques; Phosphates; Phosphorylation; Potassium Compounds; Rats; Second Messenger Systems; Serum Albumin, Bovine; Sulfonamides; Sulfuric Acid Esters; Tetraethylammonium | 1999 |