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DNA ligase is able to form a phosphodiester bond between the nucleotides on each side of the gap. [2] Phosphodiesters are negatively charged at pH 7. [5] The negative charge attracts histones, metal cations such as magnesium, and polyamines [needs citation]. Repulsion between these negative charges influences the conformation of the polynucleic ...
H 3 C(CH 2) 3 OMs + KSAc → H 3 C(CH 2) 3 SAc + KOMs H 3 C(CH 2) 3 SAc + HSMe → H 3 C(CH 2) 3 SH + MeSAc. A reaction unique to thioesters is the Fukuyama coupling, in which the thioester is coupled with an organozinc halide by a palladium catalyst to give a ketone.
An ester of a carboxylic acid.R stands for any group (typically hydrogen or organyl) and R ′ stands for any organyl group.. In chemistry, an ester is a compound derived from an acid (organic or inorganic) in which the hydrogen atom (H) of at least one acidic hydroxyl group (−OH) of that acid is replaced by an organyl group (R ′). [1]
An ester of carboxylic acid. R stands for any group (organic or inorganic) and R′ stands for organyl group. In chemistry, an ester is a compound derived from an acid (organic or inorganic) in which the hydrogen atom (H) of at least one acidic hydroxyl group (−OH) of that acid is replaced by an organyl group (−R).
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.
The process for class 1 inteins begins with an N-O or N-S shift when the side chain of the first residue (a serine, threonine, or cysteine) of the intein portion of the precursor protein nucleophilically attacks the peptide bond of the residue immediately upstream (that is, the final residue of the N-extein) to form a linear ester (or thioester) intermediate.
Furthermore, the TetM protein is found to allow aminoacyl-tRNA molecules to bind to the ribosomal acceptor site, despite being concentrated with tetracyclines that would typically inhibit such actions. The TetM protein is regarded as a ribosomal protection protein, exhibiting GTPase activity that is dependent upon ribosomes.
However, proteins can become cross-linked, most commonly by disulfide bonds, and the primary structure also requires specifying the cross-linking atoms, e.g., specifying the cysteines involved in the protein's disulfide bonds. Other crosslinks include desmosine.