Journal
CHEMICAL COMMUNICATIONS
Volume 54, Issue 19, Pages 2409-2412Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8cc01009a
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Funding
- ERC Starting Grant [ChemEpigen-715691]
- Netherlands Organization for Scientific Research [NCI-TA 731.015.202]
- World Bank Education Grant
- Spanish MINECO [CTQ2016-77558-R]
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Histone N-epsilon-lysine methylation is a widespread posttranslational modification that is specifically recognised by a diverse class of N-epsilon-methyllysine binding reader proteins. Combined thermodynamic data, molecular dynamics simulations, and quantum chemical studies reveal that reader proteins efficiently bind trimethylornithine and trimethylhomolysine, the simplest N-epsilon-trimethyllysine analogues that differ in the length of the side chain.
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