Effective strategy to assign 1H-15N heteronuclear correlation NMR signals from lysine side-chain NH3
+ groups of proteins at low temperature |
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Authors: | Alexandre Esadze Levani Zandarashvili Junji Iwahara |
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Institution: | 1. Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX, 77555-1068, USA
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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 1H-15N 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 1H and 15N resonances of NH3 + groups at low temperatures. This strategy involves two new 1H/13C/15N triple-resonance experiments for lysine side chains. Application to a protein-DNA complex is demonstrated. |
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