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Valine (symbol Val or V) [4] is an α-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), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain isopropyl group, making it a non-polar aliphatic amino acid.
^a EINECS for Valine ^a CID 71563 from PubChem ^a CID 1182 from PubChem This page was last edited on 11 April 2023, at 15:02 (UTC). Text is available ...
The 3 substrates of this enzyme are ATP, L-valine, and tRNA(Val), whereas its 3 products are AMP, diphosphate, and L-valyl-tRNA(Val). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-valine:tRNAVal ligase (AMP ...
Valinomycin is a dodecadepsipeptide, that is, it is made of twelve alternating amino acids and esters to form a macrocyclic molecule. The twelve carbonyl groups are essential for the binding of metal ions, and also for solvation in polar solvents.
Valinol can be generated by converting the carboxylic group of valine to an alcohol with a strong reducing agent such as lithium aluminium hydride, [2] or with NaBH 4 and I 2 (forming the borane–tetrahydrofuran complex). [3] In both cases the valinol produced can be subsequently purified by short path distillation.
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The vessels contain buffer solutions with different pH values, so that a pH gradient is effectively established inside the capillary. The buffer solution in each vessel has an electrical contact with a voltage divider connected to a high-voltage power supply, which establishes an electrical field along the capillary.
The 3 substrates of this enzyme are L-valine, H 2 O, and NADP +, whereas its 4 products are 3-methyl-2-oxobutanoate, NH 3, NADPH, and H +. This enzyme belongs to the family of oxidoreductases , specifically those acting on the CH-NH 2 group of donors with NAD + or NADP + as acceptor.