Impact of two-bond 15 Nā?? 15 N scalar couplings on 15 N transverse relaxation measurements for arginine side chains of proteins
Impact of two-bond 15 Nā?? 15 N scalar couplings on 15 N transverse relaxation measurements for arginine side chains of proteins
Abstract NMR relaxation of arginine (Arg) 15NĪµ nuclei is useful for studying side-chain dynamics of proteins. In this work, we studied the impact of two geminal 15Nā??15N scalar couplings on measurements of transverse relaxation rates (R 2 ) for Arg side-chain 15NĪµ nuclei. For 12 Arg side chains of the DNA-binding domain of the Antp protein, we measured the geminal 15Nā??15N couplings ( 2 J NN ) of the 15NĪµ nuclei and found that the magnitudes of the 2 J NN coupling constants were virtually uniform with an average of 1.2Ā*Hz. Our simulations, assuming ideal 180Ā° rotations for all 15N nuclei, suggested that the two 2 J NN couplings of this magnitude could in principle cause significant modulation in signal intensities during the Carrā??Purcell-Meiboomā??Gill (CPMG) scheme for Arg 15NĪµ R 2 measurements. However, our experimental data show that the expected modulation via two 2 J NN couplings vanishes during the 15N CPMG scheme. This quenching of J modulation can be explained by the mechanism described in Dittmer and Bodenhausen (Chemphyschem 7:831ā??836, 2006). This effect allows for accurate measurements of R 2 relaxation rates for Arg side-chain 15NĪµ nuclei despite the presence of two 2 J NN couplings. Although the so-called recoupling conditions may cause overestimate of R 2 rates for very mobile Arg side chains, such conditions can readily be avoided through appropriate experimental settings. Source: Journal of Biomolecular NMR |
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