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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 following other wikis use this file: Usage on bn.wikipedia.org অ্যামিনো অ্যাসিড; Usage on da.wikipedia.org Aminosyre
NH 2 and COOH termini Small arrows on one or both of the termini, or letters. For β-strands, the direction of the arrow is sufficient. Today, the direction of the polypeptide chain is often indicated by a colour ramp. Disulfide bonds Interlocked SS symbol or a zigzag, like a stylized lightning stroke. Prosthetic groups or inhibitors
In this modification, an asparagine or aspartate side chain attacks the following peptide bond, forming a symmetrical succinimide intermediate. Hydrolysis of the intermediate produces either aspartate or the β-amino acid, iso(Asp). For asparagine, either product results in the loss of the amide group, hence "deamidation". hydroxylation
The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)
Hydrogen bond: A hydrogen bond is a specific type of dipole-dipole interaction between a partially positive hydrogen atom and a partially negative electron donor that contain a pair of electrons such as oxygen, fluorine and nitrogen. The strength of hydrogen bond depends on the chemical nature and geometric arrangement of each group.
Turns are classified [2] according to the separation between the two end residues: In an α-turn the end residues are separated by four peptide bonds (i → i ± 4). In a β-turn (the most common form), by three bonds (i → i ± 3). In a γ-turn, by two bonds (i → i ± 2). In a δ-turn, by one bond (i → i ± 1), which is sterically unlikely.
The following other wikis use this file: Usage on de.wikipedia.org Peptidbindung; Usage on et.wikipedia.org Peptiidid; Usage on fi.wikipedia.org Peptidisidos