enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. 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.

  3. Denaturation (biochemistry) - Wikipedia

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

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  4. Nucleic acid thermodynamics - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_thermodynamics

    The equilibrium constant for this reaction is = [] [] []. According to the Van´t Hoff equation, the relation between free energy, ΔG, and K is ΔG° = -RTln K, where R is the ideal gas law constant, and T is the kelvin temperature of the reaction. This gives, for the nucleic acid system,

  5. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    A thermal shift assay (TSA) measures changes in the thermal denaturation temperature and hence stability of a protein under varying conditions such as variations in drug concentration, buffer formulation (pH or ionic strength), redox potential, or sequence mutation. The most common method for measuring protein thermal shifts is differential ...

  6. Buffer solution - Wikipedia

    en.wikipedia.org/wiki/Buffer_solution

    Buffer capacity rises to a local maximum at pH = pK a. The height of this peak depends on the value of pK a. Buffer capacity is negligible when the concentration [HA] of buffering agent is very small and increases with increasing concentration of the buffering agent. [3] Some authors show only this region in graphs of buffer capacity. [2]

  7. Denaturation midpoint - Wikipedia

    en.wikipedia.org/wiki/Denaturation_midpoint

    Denaturation midpoint of a protein is defined as the temperature (T m) or concentration of denaturant (C m) at which both the folded and unfolded states are equally populated at equilibrium (assuming two-state protein folding). T m is often determined using a thermal shift assay.

  8. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    The bicarbonate buffer, consisting of a mixture of carbonic acid (H 2 CO 3) and a bicarbonate (HCO − 3) salt in solution, is the most abundant buffer in the extracellular fluid, and it is also the buffer whose acid-to-base ratio can be changed very easily and rapidly. [15]

  9. Denaturation - Wikipedia

    en.wikipedia.org/wiki/Denaturation

    Denaturation (biochemistry), a structural change in macromolecules caused by extreme conditions; Denaturation (fissile materials), transforming fissile materials so that they cannot be used in nuclear weapons; Denaturation (food), intentional adulteration of food or drink rendering it unfit for consumption while remaining suitable for other uses