title: Effective strategy to assign ¹H- ¹⁵N heteronuclear correlation NMR signals from lysine side-chain NH3₃⁺ groups of proteins at low temperature.
abstract: Recent studies have shown that lysine side-chain NH3(+) groups are excellent probes for NMR investigations of dynamics involving hydrogen bonds and ion pairs relevant to protein function. However, due to rapid hydrogen exchange, observation of (1)H-(15)N NMR cross peaks from lysine NH3(+) groups often requires use of a relatively low temperature, which renders difficulty in resonance assignment. Here we present an effective strategy to assign (1)H and (15)N resonances of NH3(+) groups at low temperatures. This strategy involves two new (1)H/(13)C/(15)N triple-resonance experiments for lysine side chains. Application to a protein-DNA complex is demonstrated.
authors.affiliation: Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX, 77555-1068, USA.
authors.forename: Alexandre
authors.initials: A
authors.lastname: Esadze
authors.forename: Levani
authors.initials: L
authors.lastname: Zandarashvili
authors.forename: Junji
authors.initials: J
authors.lastname: Iwahara
mesh_terms: D064751:Ammonium Compounds / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry; D008239:Lysine / Q000737:chemistry*; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D013696:Temperature
chemical_list: D064751:Ammonium Compounds; D009587:Nitrogen Isotopes; D011506:Proteins; D006859:Hydrogen; D008239:Lysine