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tert-Butyloxycarbonyl protecting group. The tert-butyloxycarbonyl protecting group or tert-butoxycarbonyl protecting group [1] (BOC group) is an acid-labile protecting group used in organic synthesis. The BOC group can be added to amines under aqueous conditions using di-tert-butyl dicarbonate in the presence of a base such as sodium hydroxide:
For example, the amino acid tyrosine could be protected as a benzyl ester on the carboxyl group, a fluorenylmethylenoxy carbamate on the amine group, and a tert-butyl ether on the phenol group. The benzyl ester can be removed by hydrogenolysis, the fluorenylmethylenoxy group (Fmoc) by bases (such as piperidine), and the phenolic tert -butyl ...
The Boc group is removed with acid, such as trifluoroacetic acid (TFA). This forms a positively charged amino group in the presence of excess TFA (note that the amino group is not protonated in the image on the right), which is neutralized and coupled to the incoming activated amino acid. [27]
The Boc group can be added to the amine under aqueous conditions using di-tert-butyl dicarbonate in the presence of a base such as sodium bicarbonate. Protection of the amine can also be accomplished in acetonitrile solution using 4-dimethylaminopyridine (DMAP) as the base.
The fluorenylmethoxycarbonyl protecting group (Fmoc) is a base-labile amine protecting group used in organic synthesis, particularly in peptide synthesis. [1] It is popular for its stability toward acids and hydrolysis and its selective removal by weak bases, such as piperidine , without affecting most other protecting groups or sensitive ...
Blocking of reactive amino groups. This allows the internal tryptic peptides to be identified later in the process because they will be the only peptides with reactive amino groups. In this example the labelling reaction (reductive dimethylation) also blocks the reactive amino groups. Pooling. The two labeled proteomes are now mixed.
β-Alanine (beta-alanine) is a naturally occurring beta amino acid, which is an amino acid in which the amino group is attached to the β-carbon (i.e. the carbon two carbon atoms away from the carboxylate group) instead of the more usual α-carbon for alanine (α-alanine). The IUPAC name for β-alanine is 3-aminopropanoic acid.
The parent of this family of ligands is the amino acid glycine, H 2 NCH 2 COOH, in which the amino group, NH 2, is separated from the carboxyl group, COOH by a single methylene group, CH 2. When the carboxyl group is deprotonated the glycinate ion can function as a bidentate ligand , binding the metal centre through the nitrogen and one of two ...