|
Binding Constant
The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant ''K'', and is the inverse of the dissociation constant. It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: :R + L RL The reaction is characterized by the on-rate constant ''k''on and the off-rate constant ''k''off, which have units of M−1 s−1 and s−1, respectively. In equilibrium, the forward binding transition R + L → RL should be balanced by the backward unbinding transition RL → R + L. That is, :k_\,[]\,[] = k_\,[], where [R], [L] and [RL] represent the concentration of unbound free receptors, the concentration of unbound free ligand and the concentration of receptor-ligand complexes. The binding constant ''K''a is defined by :K_ = = . An often considered quantity is the dissociation constant ''K''d ≡ , which has the unit of concentration, despite the fact that str ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Equilibrium Constant
The equilibrium constant of a chemical reaction is the value of its reaction quotient at chemical equilibrium, a state approached by a dynamic chemical system after sufficient time has elapsed at which its composition has no measurable tendency towards further change. For a given set of reaction conditions, the equilibrium constant is independent of the initial analytical concentrations of the reactant and product species in the mixture. Thus, given the initial composition of a system, known equilibrium constant values can be used to determine the composition of the system at equilibrium. However, reaction parameters like temperature, solvent, and ionic strength may all influence the value of the equilibrium constant. A knowledge of equilibrium constants is essential for the understanding of many chemical systems, as well as biochemical processes such as oxygen transport by hemoglobin in blood and acid–base homeostasis in the human body. Stability constants, formation cons ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dissociation Constant
In chemistry, biochemistry, and pharmacology, a dissociation constant (K_D) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions. The dissociation constant is the inverse of the association constant. In the special case of salts, the dissociation constant can also be called an ionization constant. For a general reaction: : A_\mathit B_\mathit \mathit A + \mathit B in which a complex \ce_x \ce_y breaks down into ''x'' A subunits and ''y'' B subunits, the dissociation constant is defined as : K_D = \frac where and ''x'' B''y''are the equilibrium concentrations of A, B, and the complex A''x'' B''y'', respectively. One reason for the popularity of the dissociation constant in biochemistry and pharmacology is that in the frequently encount ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thermodynamic Activity
In chemical thermodynamics, activity (symbol ) is a measure of the "effective concentration" of a species in a mixture, in the sense that the species' chemical potential depends on the activity of a real solution in the same way that it would depend on concentration for an ideal solution. The term "activity" in this sense was coined by the American chemist Gilbert N. Lewis in 1907. By convention, activity is treated as a dimensionless quantity, although its value depends on customary choices of standard state for the species. The activity of pure substances in condensed phases (solid or liquids) is normally taken as unity (the number 1). Activity depends on temperature, pressure and composition of the mixture, among other things. For gases, the activity is the effective partial pressure, and is usually referred to as fugacity. The difference between activity and other measures of concentration arises because the interactions between different types of molecules in non-ideal gas ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gibbs Free Energy
In thermodynamics, the Gibbs free energy (or Gibbs energy; symbol G) is a thermodynamic potential that can be used to calculate the maximum amount of work that may be performed by a thermodynamically closed system at constant temperature and pressure. It also provides a necessary condition for processes such as chemical reactions that may occur under these conditions. The Gibbs free energy change , measured in joules in SI) is the ''maximum'' amount of non-expansion work that can be extracted from a closed system (one that can exchange heat and work with its surroundings, but not matter) at fixed temperature and pressure. This maximum can be attained only in a completely reversible process. When a system transforms reversibly from an initial state to a final state under these conditions, the decrease in Gibbs free energy equals the work done by the system to its surroundings, minus the work of the pressure forces. The Gibbs energy is the thermodynamic potential that is minim ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Affinity (pharmacology)
In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. The etymology stems from ''ligare'', which means 'to bind'. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein. The binding typically results in a change of conformational isomerism (conformation) of the target protein. In DNA-ligand binding studies, the ligand can be a small molecule, ion, or protein which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure. Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces. The association or docking is actually reversible through dissociation. Measurably irreversible covalent bonding between a ligand and target molecule is atypical in biological systems. In contrast to the definition of liga ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ideal Gas Constant
The molar gas constant (also known as the gas constant, universal gas constant, or ideal gas constant) is denoted by the symbol or . It is the molar equivalent to the Boltzmann constant, expressed in units of energy per temperature increment per amount of substance, i.e. the pressure–volume product, rather than energy per temperature increment per ''particle''. The constant is also a combination of the constants from Boyle's law, Charles's law, Avogadro's law, and Gay-Lussac's law. It is a physical constant that is featured in many fundamental equations in the physical sciences, such as the ideal gas law, the Arrhenius equation, and the Nernst equation. The gas constant is the constant of proportionality that relates the energy scale in physics to the temperature scale and the scale used for amount of substance. Thus, the value of the gas constant ultimately derives from historical decisions and accidents in the setting of units of energy, temperature and amount of substance ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Binding Coefficient
In medicinal chemistry and pharmacology, a binding coefficient is a quantity representing the extent to which a chemical compound will bind to a macromolecule. The preferential binding coefficient can be derived from the Kirkwood-Buff solution theory of solutions. Preferential binding is defined as a thermodynamic expression that describes the binding of the cosolvent over the solvent. This is in a system that is open to both the solvent and cosolvent. Consequently, preferential interaction coefficients are measures of interactions that involve “solutes that participate in a reaction in solution.” Thomas Record Jr. M, Anderson CF. (1995"Interpretation of Preferential Interaction Coefficients of Nonelectrolytes and of Electrolyte Ions in Terms of a Two-Domain Model."''Biophysical Journal.'' 68:786-794. See also * Binding constant * Partition coefficient * Binding affinity In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
