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1. Metabolomic Analysis Reveals That the Drosophila Gene lysine  Influences Diverse Aspects of Metabolism

   https://doi.org/10.1534/genetics.117.300201  

   St. Clair, Samantha L.; Li, Hongde; Ashraf, Usman; Karty, Jonathan A.; Tennessen, Jason M. (December 2017, Genetics)
2. Unnatural Lysines with Reduced Sidechain N ‐Basicity: Synthesis of N ‐trifluoroethyl Substituted Lysine and Homologs

   https://doi.org/10.1002/slct.202203132  

   Jameson, Brian; Glaser, Rainer (December 2022, ChemistrySelect)

   Abstract The syntheses are reported of N^ϵ‐(2,2,2‐trifluoroethyl)‐D,L‐lysine (^tFK) and N^ζ‐(2,2,2‐trifluoroethyl)‐D,L‐homolysine (^tFK₊₁) from amino alcohols HO−(CH₂)_n−NH₂. The syntheses involve reductive amination, Appel bromination, and the stereoselective bond formation between C_α of the amino acid and the fluorinated alkyl chain in the Schöllkopf bislactim amino acid synthesis. The methyl esters of the fluorinated amino acids are the relevant substrates for oligopeptide synthesis. With theR‐Schöllkopf reagent, we stereoselectively generated methyl N^ϵ‐boc‐N^ϵ‐(2,2,2‐trifluoroethyl)‐L‐lysinate and methyl N^ζ‐boc‐N^ζ‐(2,2,2‐trifluoroethyl)‐L‐homolysinate. Products and intermediates were characterized by ¹H NMR, ¹³C NMR, COSY, HSQC, and LCMS. A variety of N‐functionality may be introduced by reacting hemiacetals with different appendages. This fluorine modification reduces the sidechain N‐basicity by combined ‐I effect of the three fluorines. This effect increases the [amine]/[ammonium ion] ratio of the sidechain amine in lysine to facilitate carbamylation at lower pH conditions. 

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3. Rational Design of Dimeric Lysine N -Alkylamides as Potent and Broad-Spectrum Antibacterial Agents

   https://doi.org/10.1021/acs.jmedchem.7b01704  

   Niu, Youhong; Wang, Minghui; Cao, Yafei; Nimmagadda, Alekhya; Hu, Jianxing; Wu, Yanfen; Cai, Jianfeng; Ye, Xin-Shan (March 2018, Journal of Medicinal Chemistry)
4. ParB C-terminal lysine residues are essential for dimerization, in vitro DNA sliding and in vivo function

   https://doi.org/10.1101/2025.06.10.659001  

   Aleshintsev, Aleksey; Way, Linsey E; Guerra, Bianca; Serwaa, Lois Akosua; Molina, Miranda; Wang, Xindan; Kim, HyeongJun (June 2025, bioRxiv)

   ABSTRACT The broadly conserved ParB protein performs crucial functions in bacterial chromosome segregation and replication regulation. The cellular function of ParB requires it to dimerize, recognizeparSDNA sequences, clamp on DNA, then slide to adjacent sequences through nonspecific DNA binding. How ParB coordinates nonspecific DNA binding and sliding remains elusive. Here, we combine multiplein vitrobiophysical and computational tools andin vivoapproaches to address this question. We found that the five conserved lysine residues in the C-terminal domain of ParB play distinct roles in proper positioning and sliding on DNA, and their integrity is crucial for ParB’sin vivofunctions. Many proteins with diverse cellular activities need to move on DNA while loosely bound. Our findings reveal the detailed molecular mechanism by which multiple flexible basic residues enable DNA binding proteins to efficiently slide along DNA. 

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5. Dynamics of Lysine as a Heme Axial Ligand: NMR Analysis of the Chlamydomonas reinhardtii Hemoglobin THB1

   https://doi.org/10.1021/acs.biochem.6b00926  

   Preimesberger, Matthew R.; Majumdar, Ananya; Lecomte, Juliette T. (January 2017, Biochemistry)