Search results
Results from the WOW.Com Content Network
Aspartic acid ball and stick model spinning. Aspartic acid (symbol Asp or D; [4] the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins. [5] The L-isomer of aspartic acid is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins.
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 pK a values of an amino acid side chain in solution is typically inferred from the pK a values of model compounds (compounds that are similar to the ...
Amino acid Short Abbrev. Side chain Hydro-phobic pKa § Polar pH Small Tiny Aromatic or Aliphatic van der Waals volume (Å 3) Alanine: A Ala -CH 3 - - Aliphatic 67 Cysteine: C Cys -CH 2 SH: 8.55 acidic - 86 Aspartic acid: D Asp -CH 2 COOH 3.67 acidic - 91 Glutamic acid: E Glu -CH 2 CH 2 COOH 4.25 acidic - 109 Phenylalanine: F Phe -CH 2 C 6 H 5 ...
The N-O distance required is less than 4 Å (400 pm). Amino acids greater than this distance apart do not qualify as forming a salt bridge. [11] Due to the numerous ionizable side chains of amino acids found throughout a protein, the pH at which a protein is placed is crucial to its stability.
Main page; Contents; Current events; Random article; About Wikipedia; Contact us
Two amino acids have acidic side chains at physiological pH (aspartate or glutamate) and so are the most common members of the acidic triad residue. [3] Cytomegalovirus protease [ b ] uses a pair of histidines, one as the base, as usual, and one as the acid. [ 1 ]
Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains. Typically, a carbohydrate tree can solely be added to an asparagine residue if the latter is flanked on the C side by X-serine or X-threonine, where X is any amino acid with the exception of proline. [19]
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 ...