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In organic chemistry, a thiol (/ ˈ θ aɪ ɒ l /; [1] from Ancient Greek θεῖον (theion) 'sulfur' [2]), or thiol derivative, is any organosulfur compound of the form R−SH, where R represents an alkyl or other organic substituent. The −SH functional group itself is referred to as either a thiol group or a sulfhydryl group, or a ...
Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another.
Structure of acetyl coenzyme A, a thioester that is a key intermediate in the biosynthesis of many biomolecules. Thioesters are common intermediates in many biosynthetic reactions, including the formation and degradation of fatty acids and mevalonate , precursor to steroids.
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...
The conjugate base of thioacetic acid, thioacetate, is a reagent used for installing thiol groups via the displacement of alkyl halides by a two-step process. The halide is displaced to give a thioester intermedate, which is then hydrolyzed: R−X + CH 3 COS − → R−SC(O)CH 3 + X − R−SC(O)CH 3 + H 2 O → R−SH + CH 3 CO 2 H
[4] [5] The amide group is called a peptide bond when it is part of the main chain of a protein, and an isopeptide bond when it occurs in a side chain, as in asparagine and glutamine. It can be viewed as a derivative of a carboxylic acid ( R−C(=O)−OH ) with the hydroxyl group ( −OH ) replaced by an amine group ( −NR′R″ ); or ...
Cysteine (symbol Cys or C; [5] / ˈ s ɪ s t ɪ iː n /) [6] is a semiessential [7] proteinogenic amino acid with the formula HOOC−CH(−NH 2)−CH 2 −SH.The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile.