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In organic chemistry, the Mannich reaction is a three-component organic reaction that involves the amino alkylation of an acidic proton next to a carbonyl (C=O) functional group by formaldehyde (H−CHO) and a primary or secondary amine (−NH 2) or ammonia (NH 3). [1] The final product is a β-amino-carbonyl compound also known as a Mannich base.
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 ...
These hydrides facilitate the reduction of imines or iminium ions—key intermediates in reductive amination—into secondary or tertiary amines. This reaction typically occurs under mild conditions with excellent selectivity, which often makes H 2 /Pd the first choice for synthesizing amines in pharmaceuticals and fine chemicals.
This secondary structure then folds to produce the tertiary structure of the protein. The tertiary structure is the proteins overall 3D structure which is made of different secondary structures folding together. In the tertiary structure, key protein features e.g. the active site, are folded and formed enabling the protein to function.
In order to optimize synthesis of long peptides, a method was developed in Medicon Valley for converting peptide sequences. [citation needed] The simple pre-sequence (e.g. Lysine (Lysn); Glutamic Acid (Glun); (LysGlu)n) that is incorporated at the C-terminus of the peptide to induce an alpha-helix-like structure.
The primary structure of a protein refers to the sequence of amino acids in the polypeptide chain. The primary structure is held together by peptide bonds that are made during the process of protein biosynthesis.
The synthesis of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is feed-back inhibited by lysine, isoleucine, and threonine, which prevents the synthesis of the amino acids derived from aspartate. So, in addition to inhibiting the first enzyme of the aspartate ...
A second type of transamination reaction can be described as a nucleophilic substitution of one amine or amide anion on an amine or ammonium salt. [1] For example, the attack of a primary amine by a primary amide anion can be used to prepare secondary amines: RNH 2 + R'NH − → RR'NH + NH 2 −