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The oxidation pathway starts with the removal of the amino group by a transaminase; the amino group is then fed into the urea cycle. The other product of transamidation is a keto acid that enters the citric acid cycle. [79] Glucogenic amino acids can also be converted into glucose, through gluconeogenesis. [80]
Printable version; In other projects Wikidata item; Appearance. move to sidebar hide. Amino acids are listed by type: Proteinogenic amino acid; Non-proteinogenic ...
The foodstuffs listed for comparison show the essential amino acid content per unit of the total protein of the food, 100g of spinach, for example, only contains 2.9g of protein (6% Daily Value), and of that protein 1.36% is tryptophan. [2] [7] (note that the examples have not been corrected for digestibility)
Printable version; In other projects ... This is a list of articles that describe particular biomolecules or types of biomolecules. A. For ... Amino acid; Amylase ...
Aromatic amino acids, excepting histidine, absorb ultraviolet light above and beyond 250 nm and will fluoresce under these conditions. This characteristic is used in quantitative analysis, notably in determining the concentrations of these amino acids in solution. [1] [2] Most proteins absorb at 280 nm due to the presence of tyrosine and ...
Below is a list organised by food group and given in measurements of grams of protein per 100 grams of food portion. The reduction of water content has the greatest effect of increasing protein as a proportion of the overall mass of the food in question. Not all protein is equally digestible.
Lysine. Technically, any organic compound with an amine (–NH 2) and a carboxylic acid (–COOH) functional group is an amino acid. The proteinogenic amino acids are a small subset of this group that possess a central carbon atom (α- or 2-) bearing an amino group, a carboxyl group, a side chain and an α-hydrogen levo conformation, with the exception of glycine, which is achiral, and proline ...
The N-terminal amino group of a polypeptide can be modified covalently, e.g., Fig. 1 N-terminal acetylation. acetylation (=) The positive charge on the N-terminal amino group may be eliminated by changing it to an acetyl group (N-terminal blocking). formylation (=)