Effective strategy to assign <sup>1</sup>H-<sup>15</sup>N heteronuclear correlation NMR signals from lysine side-chain NH<inf>3</inf> <sup>+</sup> groups of proteins at low temperature

Alexandre Esadze, Levani Zandarashvili, Junji Iwahara

    Research output: Contribution to journalArticle

    14 Citations (Scopus)

    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.

    Original languageEnglish (US)
    Pages (from-to)23-27
    Number of pages5
    JournalJournal of Biomolecular NMR
    Volume60
    Issue number1
    DOIs
    StatePublished - 2014

    Fingerprint

    Biomolecular Nuclear Magnetic Resonance
    Lysine
    Nuclear magnetic resonance
    Temperature
    Pair Bond
    Proteins
    Protons
    Hydrogen
    Hydrogen bonds
    Observation
    Ions
    DNA
    Experiments

    Keywords

    • H/C/N resonances
    • Lysine
    • NH groups
    • Proteins
    • Side chains

    ASJC Scopus subject areas

    • Biochemistry
    • Spectroscopy

    Cite this

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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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    T1 - Effective strategy to assign 1H-15N heteronuclear correlation NMR signals from lysine side-chain NH3 + groups of proteins at low temperature

    AU - Esadze, Alexandre

    AU - Zandarashvili, Levani

    AU - Iwahara, Junji

    PY - 2014

    Y1 - 2014

    N2 - 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.

    AB - 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.

    KW - H/C/N resonances

    KW - Lysine

    KW - NH groups

    KW - Proteins

    KW - Side chains

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