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  2. Steady state (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Steady_state_(biochemistry)

    In biochemistry, steady state refers to the maintenance of constant internal concentrations of molecules and ions in the cells and organs of living systems. [1] Living organisms remain at a dynamic steady state where their internal composition at both cellular and gross levels are relatively constant, but different from equilibrium concentrations. [1]

  3. Chemical equilibrium - Wikipedia

    en.wikipedia.org/wiki/Chemical_equilibrium

    If a dynamic equilibrium is disturbed by changing the conditions, the position of equilibrium moves to partially reverse the change. For example, adding more S (to the chemical reaction above) from the outside will cause an excess of products, and the system will try to counteract this by increasing the reverse reaction and pushing the ...

  4. Determination of equilibrium constants - Wikipedia

    en.wikipedia.org/wiki/Determination_of...

    The equilibrium expression above is a function of the concentrations [A], [B] etc. of the chemical species in equilibrium. The equilibrium constant value can be determined if any one of these concentrations can be measured.

  5. Dissociation constant - Wikipedia

    en.wikipedia.org/wiki/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.

  6. Steady state (chemistry) - Wikipedia

    en.wikipedia.org/wiki/Steady_state_(chemistry)

    The steady state approximation, [1] occasionally called the stationary-state approximation or Bodenstein's quasi-steady state approximation, involves setting the rate of change of a reaction intermediate in a reaction mechanism equal to zero so that the kinetic equations can be simplified by setting the rate of formation of the intermediate equal to the rate of its destruction.

  7. Binding selectivity - Wikipedia

    en.wikipedia.org/wiki/Binding_selectivity

    The concept of selectivity is used to quantify the extent to which one chemical substance, A, binds each of two other chemical substances, B and C. The simplest case is where the complexes formed have 1:1 stoichiometry. Then, the two interactions may be characterized by equilibrium constants K AB and K AC.

  8. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.

  9. Dynamic equilibrium - Wikipedia

    en.wikipedia.org/wiki/Dynamic_equilibrium

    In a new bottle of soda, the concentration of carbon dioxide in the liquid phase has a particular value. If half of the liquid is poured out and the bottle is sealed, carbon dioxide will leave the liquid phase at an ever-decreasing rate, and the partial pressure of carbon dioxide in the gas phase will increase until equilibrium is reached.