Related Experiment Video
Updated: Mar 14, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
Published on: November 29, 2014
Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an
Yan-Jiun Lee1, M J Schmidt2, Jeffery M Tharp1
1Department of Chemistry, Texas A&M University, College Station, TX 7743, USA. wliu@chem.tamu.edu.
Abstract:
Fluorophenylalanines bearing 2-5 fluorine atoms at the phenyl ring have been genetically encoded by amber codon. Replacement of F59, a phenylalanine residue that is directly involved in interactions with trimethylated K9 of histone H3, in the Mpp8 chromodomain recombinantly with fluorophenylalanines significantly impairs the binding to a K9-trimethylated H3 peptide.
More Related Videos
Related Concept Videos
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
Spreading of Chromatin Modifications
Writers
The writer...
Epigenetic Regulation
X-chromosome...
Epigenetic Regulation
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....

