Mimic Aids Study Of Protein Acetylation | July 19, 2010 Issue - Vol. 88 Issue 29 | Chemical & Engineering News
Volume 88 Issue 29 | p. 32 | Concentrates
Issue Date: July 19, 2010

Mimic Aids Study Of Protein Acetylation

Derivatizing cysteines to create a mimic of acetyl-lysine groups could be useful in biochemistry
Department: Science & Technology
News Channels: JACS In C&EN
Keywords: acetylation, phosphorylation, post-translational modification

Like protein phosphorylation, acetylation of lysine residues on proteins may have an important regulatory role in cell pathways. Thousands of mammalian proteins are naturally acetylated, but it’s technically difficult to acetylate lysine groups in the lab, complicating the study of the functional consequences of acetylation. Philip A. Cole of Johns Hopkins University School of Medicine and coworkers have now developed an easier method: derivatizing cysteines with methylthiocarbonyl-aziridine (MTCA) to create a thiocarbamate mimic . . .

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