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The Henderson–Hasselbalch equation can be used to model these equilibria. It is important to maintain this pH of 7.4 to ensure enzymes are able to work optimally. [10] Life threatening Acidosis (a low blood pH resulting in nausea, headaches, and even coma, and convulsions) is due to a lack of functioning of enzymes at a low pH. [10]
It is very difficult to measure pH values of less than two in aqueous solution with a glass electrode, because the Nernst equation breaks down at such low pH values. To determine p K values of less than about 2 or more than about 11 spectrophotometric [ 60 ] [ 61 ] or NMR [ 62 ] [ 63 ] measurements may be used instead of, or combined with, pH ...
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 ...
k H CO 2 is a constant including the solubility of carbon dioxide in blood. k H CO 2 is approximately 0.03 (mmol/L)/mmHg; p CO 2 is the partial pressure of carbon dioxide in the blood; Combining these equations results in the following equation relating the pH of blood to the concentration of bicarbonate and the partial pressure of carbon ...
K ow, being a type of partition coefficient, serves as a measure of the relationship between lipophilicity (fat solubility) and hydrophilicity (water solubility) of a substance. The value is greater than one if a substance is more soluble in fat-like solvents such as n-octanol, and less than one if it is more soluble in water.
At pH 1 or lower, the phosphoric acid is practically undissociated. Around pH 4.7 (mid-way between the first two pK a values) the dihydrogen phosphate ion, [H 2 PO 4] −, is practically the only species present. Around pH 9.8 (mid-way between the second and third pK a values) the monohydrogen phosphate ion, [HPO 4] 2−, is the only species ...
Since Tris' pKa is more strongly temperature dependent, its use is not recommended in biochemical applications requiring consistent pH over a range of temperatures. Moreover, the temperature dependance of the pKa (and in turn buffer solution pH) makes pH adjustment difficult. [8] (E.g., the 'room temperature' pH adjustment would not translate ...
The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...