Lysine-cysteine NOS bonds: Difference between revisions
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<StructureSection size='350' side='right' caption='' scene='88/883792/6zx4_nos/ | <StructureSection size='350' side='right' caption='' scene='88/883792/6zx4_nos/2'> | ||
Lysine-cysteine "Nitrogen-Oxygen-Sulfur" (NOS) bonds 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. Disulfide bonds are a far more common type of covalent linkages between polypeptide chains. | Lysine-cysteine "Nitrogen-Oxygen-Sulfur" (NOS) bonds 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. Disulfide bonds are a far more common type of covalent linkages between polypeptide chains. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 02:10, 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. Disulfide bonds are a far more common type of covalent linkages between polypeptide chains.
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