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Center for Integrated Protein Science at the Department of Chemistry, Ludwig-Maximilians-Universität, Munich, Butenandtstraße 5-13, Munich, Germany
; Fax: +49 (0)89 2180 77756
; Tel: +49 (0)89 2180 77750
Chem. Commun., 2013,49, 379-381
29 Oct 2012,
14 Nov 2012
First published online
15 Nov 2012
Recently new lysine modifications were detected in histones and other proteins. Using the pyrrolysine amber suppression system we genetically inserted three of the new amino acids ε-N-propionyl-, ε-N-butyryl-, and ε-N-crotonyl-lysine site specifically into histone H3. The lysine at position 9 (H3 K9), which is known to be highly modified in chromatin, was replaced by these unnatural amino acids.
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