NMR paper Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.

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[NMR paper] Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.

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08-19-2014, 11:21 AM

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Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.

Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.

Related Articles Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.

J Biomol NMR. 2014 Aug 17;

Authors: Esadze A, Zandarashvili L, Iwahara J

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.

PMID: 25129623 [PubMed - as supplied by publisher]

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