Lysine-cysteine NOS bonds: Difference between revisions
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Lysine-cysteine "Nitrogen-Oxygen-Sulfur" (NOS) bonds (<scene name='88/883792/6zx4_nos/2'>restore initial scene</scene>) were first reported in 2021 in transaldolases<ref name="wensien2021">PMID: 33953398</ref>. The sidechains of a lysine and a cysteine, joined by an NOS bond, make a covalent linkage between polypeptide chains. The [[disulfide bond]] is a far more common type of covalent linkage between polypeptide chains. | Lysine-cysteine "Nitrogen-Oxygen-Sulfur" (NOS) bonds (<scene name='88/883792/6zx4_nos/2'>restore initial scene</scene>) were first reported in 2021 in transaldolases<ref name="wensien2021">PMID: 33953398</ref>. The sidechains of a lysine and a cysteine, joined by an NOS bond, make a covalent linkage between polypeptide chains. The [[disulfide bond]] is a far more common type of covalent linkage between polypeptide chains. | ||
<scene name='88/883792/6zx4_nos_whole_molecule/1'>The NOS bond is located</scene> near the N-terminus of the 352 amino acid chain, between Lys8 and Cys38, near the surface. | |||
</StructureSection> | </StructureSection> |
Revision as of 02:38, 26 May 2021
Lysine-cysteine "Nitrogen-Oxygen-Sulfur" (NOS) bonds () were first reported in 2021 in transaldolases[1]. The sidechains of a lysine and a cysteine, joined by an NOS bond, make a covalent linkage between polypeptide chains. The disulfide bond is a far more common type of covalent linkage between polypeptide chains. near the N-terminus of the 352 amino acid chain, between Lys8 and Cys38, near the surface.
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