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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.
[10] [11] This method avoids needing the amine to initiate an amide-forming acyl substitution but does requires synthesis and handling of the unstable thiocarboxylic acid. [11] Unlike the Schmidt reaction or other nucleophilic-attack pathways, reaction with an aryl or alkyl azide begins with a [3+2] cycloaddition .
[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 ...
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.
[11] [12] A trichlorosilane based "head group", for example in a FDTS molecule, reacts with a hydroxyl group on a substrate, and forms very stable, covalent bond [R-Si-O-substrate] with an energy of 452 kJ/mol. Thiol-metal bonds are on the order of 100 kJ/mol, making them fairly stable in a variety of temperatures, solvents, and potentials. [10]
In native chemical ligation, the ionized thiol group of an N-terminal cysteine residue of an unprotected peptide attacks the C-terminal thioester of a second unprotected peptide, in an aqueous buffer at pH 7.0 and room temperature. This transthioesterification step is reversible in the presence of an aryl thiol catalyst, rendering the reaction ...