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  2. 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]

  3. Reduction potential - Wikipedia

    en.wikipedia.org/wiki/Reduction_potential

    In aqueous solutions, redox potential is a measure of the tendency of the solution to either gain or lose electrons in a reaction. A solution with a higher (more positive) reduction potential than some other molecule will have a tendency to gain electrons from this molecule (i.e. to be reduced by oxidizing this other molecule) and a solution with a lower (more negative) reduction potential ...

  4. Table of standard reduction potentials for half-reactions ...

    en.wikipedia.org/wiki/Table_of_standard...

    It is therefore important to know to what exact definition does refer the value of a reduction potential for a given biochemical redox process reported at pH = 7, and to correctly understand the relationship used. Is it simply: = calculated at pH 7 (with or without corrections for the activity coefficients),

  5. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    The isoelectric point (pI, pH(I), IEP), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH(I). [1] However, pI is also used. [2] For brevity, this article uses pI.

  6. 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.

  7. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    The hyperchromic effect is the striking increase in absorbance of DNA upon denaturation. The two strands of DNA are bound together mainly by the stacking interactions, hydrogen bonds and hydrophobic effect between the complementary bases. The hydrogen bond limits the resonance of the aromatic ring so the absorbance of the sample is limited as well.

  8. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    Important parameters to consider are temperature, which should be less than 0 °C to avoid denaturation, pH and protein concentration in solution. Miscible organic solvents decrease the dielectric constant of water, which in effect allows two proteins to come close together.

  9. pH - Wikipedia

    en.wikipedia.org/wiki/PH

    The electrode potential is proportional to pH when pH is defined in terms of activity. The precise measurement of pH is presented in International Standard ISO 31-8 as follows: [ 15 ] A galvanic cell is set up to measure the electromotive force (e.m.f.) between a reference electrode and an electrode sensitive to the hydrogen ion activity when ...