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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. Freshwater environmental quality parameters - Wikipedia

    en.wikipedia.org/wiki/Freshwater_environmental...

    The toxicity of ammonia is dependent on both pH and temperature and an added complexity is the buffering effect of the blood/water interface across the gill membrane which masks any additional toxicity over about pH 8.0. The management of river chemistry to avoid ecological damage is particularly difficult in the case of ammonia as a wide range ...

  4. 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.

  5. Freshwater acidification - Wikipedia

    en.wikipedia.org/wiki/Freshwater_acidification

    Diagram depicting the sources and cycles of acid rain precipitation. Freshwater acidification occurs when acidic inputs enter a body of fresh water through the weathering of rocks, invasion of acidifying gas (e.g. carbon dioxide), or by the reduction of acid anions, like sulfate and nitrate within a lake, pond, or reservoir. [1]

  6. 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.

  7. 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.

  8. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    The pI value can affect the solubility of a molecule at a given pH. Such molecules have minimum solubility in water or salt solutions at the pH that corresponds to their pI and often precipitate out of solution. Biological amphoteric molecules such as proteins contain both acidic and basic functional groups. Amino acids that make up proteins ...

  9. Buffer solution - Wikipedia

    en.wikipedia.org/wiki/Buffer_solution

    A buffer solution is a solution where the pH does not change significantly on dilution or if an acid or base is added at constant temperature. [1] Its pH changes very little when a small amount of strong acid or base is added to it. Buffer solutions are used as a means of keeping pH at a nearly constant value in a wide variety of chemical ...