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Histidine ball and stick model spinning. Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated –NH 3 + form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially ...
Acid–base imbalance occurs when a significant insult causes the blood pH to shift out of the normal range (7.32 to 7.42 [16]). An abnormally low pH in the extracellular fluid is called an acidemia and an abnormally high pH is called an alkalemia. [citation needed]
The triad of cytomegalovirus protease [b] uses histidine as both the acid and base triad members. Removing the acid histidine results in only a 10-fold activity loss (compared to >10,000-fold when aspartate is removed from chymotrypsin). This triad has been interpreted as a possible way of generating a less active enzyme to control cleavage ...
The normal concentration of 3-methylhistidine in the urine of healthy adult humans has been detected and quantified in a range of 3.63–69.27 micromoles per millimole (μmol/mmol) of creatinine, with most studies reporting the average urinary concentration between 15 and 20 μmol/mmol of creatinine. [1]
A smaller H + concentration means a greater OH − concentration and, therefore, a greater K b and a greater pH. NaOH (s) (sodium hydroxide) is a stronger base than (CH 3 CH 2) 2 NH (l) (diethylamine) which is a stronger base than NH 3 (g) (ammonia). As the bases get weaker, the smaller the K b values become. [1]
The compound added at high concentration replaces virtually all carrier-bound protein which is thus eluted from the carrier. Imidazole is the side chain of histidine and is typically used at a concentration of 150 - 500 mM for elution. Histidine or histamine can also be used. Decrease in pH
When a protein folds, the titratable amino acids in the protein are transferred from a solution-like environment to an environment determined by the 3-dimensional structure of the protein. For example, in an unfolded protein, an aspartic acid typically is in an environment which exposes the titratable side chain to water.
If the pH is known, the ratio may be calculated. This ratio is independent of the analytical concentration of the acid. In water, measurable pK a values range from about −2 for a strong acid to about 12 for a very weak acid (or strong base). A buffer solution of a desired pH can be prepared as a mixture of a weak acid and its conjugate base ...