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For amino acids with uncharged side-chains the zwitterion predominates at pH values between the two pK a values, but coexists in equilibrium with small amounts of net negative and net positive ions. At the midpoint between the two p K a values, the trace amount of net negative and trace of net positive ions balance, so that average net charge ...
There, most of the peptides are broken into single amino acids. Absorption of the amino acids and their derivatives into which dietary protein is degraded is done by the gastrointestinal tract. The absorption rates of individual amino acids are highly dependent on the protein source; for example, the digestibilities of many amino acids in ...
AAindex is a database of amino acid indices, amino acid mutation matrices, and pair-wise contact potentials. [ 1 ] [ 2 ] The data represent various physicochemical and biochemical properties of amino acids and pairs of amino acids.
Amino acids that must be obtained from the diet are called essential amino acids. Eukaryotes can synthesize some of the amino acids from other substrates . Consequently, only a subset of the amino acids used in protein synthesis are essential nutrients .
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)
A codon table can be used to translate a genetic code into a sequence of amino acids. [1] [2] The standard genetic code is traditionally represented as an RNA codon table, because when proteins are made in a cell by ribosomes, it is messenger RNA (mRNA) that directs protein synthesis. [2] [3] The mRNA sequence is determined by the sequence of ...
Amino acids produced from the same precursors also had widely varying compositions. It is difficult to explain these trends because of limited data on the kinetic isotope effects associated with reactions that synthesize amino acid carbon skeletons. Nevertheless, some insights can be gained by applying the logic above to the reaction networks ...
A table comparing four different scales for the hydrophobicity of an amino acid residue in a protein with the most hydrophobic amino acids on the top. A number of different hydrophobicity scales have been developed. [3] [1] [7] [8] [9] The Expasy Protscale website lists a total of 22 hydrophobicity scales. [10]