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Homotaurine (also known as tramiprosate , 3-amino-1-propanesulfonic acid, or 3-APS) is a natural sulfonic acid found in seaweed. [3] It is analogous to taurine, but with an extra carbon in its chain. It has GABAergic activity, apparently by mimicking GABA, which it resembles. [4]
Also, amino acid side chain affinity for water was measured using vapor phases. [14] Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. [ 18 ] The hydration potential and its correlation to the appearance of amino acids on the surface of proteins was studied by Wolfenden.
A conservative replacement (also called a conservative mutation or a conservative substitution or a homologous replacement) is an amino acid replacement in a protein that changes a given amino acid to a different amino acid with similar biochemical properties (e.g. charge, hydrophobicity and size). [1] [2]
Trimethylglycine is an amino acid derivative with the formula (CH 3) 3 N + CH 2 CO − 2.A colorless, water-soluble solid, it occurs in plants. [5] Trimethylglycine is a zwitterion: the molecule contains both a quaternary ammonium group and a carboxylate group.
Backbone-dependent rotamer library for serine.Each plot shows the population of the χ 1 rotamers of serine as a function of the backbone dihedral angles φ and ψ. In biochemistry, a backbone-dependent rotamer library provides the frequencies, mean dihedral angles, and standard deviations of the discrete conformations (known as rotamers) of the amino acid side chains in proteins as a function ...
Deamidation is a chemical reaction in which an amide functional group in the side chain of the amino acids asparagine or glutamine is removed or converted to another functional group. Typically, asparagine is converted to aspartic acid or isoaspartic acid. Glutamine is converted to glutamic acid or pyroglutamic acid (5-oxoproline).
Most of the organic acidemias result from defective autosomal genes for various enzymes important to amino acid metabolism.Neurological and physiological harm is caused by this impaired ability to synthesize a key enzyme required to break down a specific amino acid, or group of amino acids, resulting in acidemia and toxicity to specific organs systems.
Selenomethionine (SeMet) is a naturally occurring amino acid.The L-selenomethionine enantiomer is the main form of selenium found in Brazil nuts, cereal grains, soybeans, and grassland legumes, while Se-methylselenocysteine, or its γ-glutamyl derivative, is the major form of selenium found in Astragalus, Allium, and Brassica species. [1]