ArticleJournal of biomolecular NMR2005
Measurement of eight scalar and dipolar couplings for methine-methylene pairs in proteins and nucleic acids.
Article in Journal of biomolecular NMR, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 34 citations in OpenAlex.
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- Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3.Data in brief · 2015Article
- ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB.Journal of chemical theory and computation · 2015Article
- Stereospecific assignments in proteins using exact NOEs.Journal of biomolecular NMR · 2013Article
- Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks.Journal of biomolecular NMR · 2013Article
- The Polarizable Atomic Multipole-based AMOEBA Force Field for Proteins.Journal of chemical theory and computation · 2013Article
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- Direct detection of CH/pi interactions in proteins.Nature chemistry · 2010Article
- Side chain: backbone projections in aromatic and ASX residues from NMR cross-correlated relaxation.Journal of biomolecular NMR · 2010Article
- An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein.Journal of biomolecular NMR · 2009Article
- Liquid-crystal NMR structure of HIV TAR RNA bound to its SELEX RNA aptamer reveals the origins of the high stability of the complex.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Characterizing the relative orientation and dynamics of RNA A-form helices using NMR residual dipolar couplings.Nature protocols · 2007Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
A new 3D, spin-state-selective coherence transfer NMR experiment is described that yields accurate measurements for eight scalar or dipolar couplings within a spin system composed of a methylene adjacent to a methine group. Implementations of the experiment have been optimized for proteins and for nucleic acids. The experiments are demonstrated for Cbeta-Calpha moieties of the third IgG-binding domain from Streptococcal Protein G (GB3) and for C5'-C4' groups in a 24-nt RNA oligomer. Chemical shifts of Calpha, Cbeta and Hbeta (respectively C4', C5' and H5') are dispersed in the three orthogonal dimensions, and the absence of heteronuclear decoupling leads to distinct and well-resolved E.COSY multiplet patterns. In an isotropic sample, the E.COSY displacements correspond to 1J(CalphaHalpha), 2J(CalphaHbeta2)+2J(CalphaHbeta3), 2J(CbetaHalpha), 1J(CbetaHbeta2)+1J(CbetaHbeta3), 1J(CbetaHbeta2)-2J(Hbeta2Hbeta3), 1J(CbetaHbeta3)-2J(Hbeta2Hbeta3), 3J(HalphaHbeta2) and 3J(HalphaHbeta3) for proteins, and 1J(C4'H4'), 2J(C4'H5')+2J(C4'H5"), 2J(C5'H4'), 1J(C5'H5')+1J(C5'H5"), 1J(C5'H5')-2J(H5'H5"), 1J(C5'H5")-2J(H5'H5"), 3J(H4'H5') and 3J(H4'H5") in nucleic acids. The experiment, based on relaxation-optimized spectroscopy, yields best results when applied to residues where the methine-methylene group corresponds to a reasonably isolated spin system, as applies for C, F, Y, W, D, N and H residues in proteins, or the C5'-C4' groups in nucleic acids. Splittings can be measured under either isotropic or weakly aligned conditions, yielding valuable structural information both through the 3J couplings and the one-, two- and three-bond dipolar interactions. Dipolar couplings for 10 out of 13 sidechains in GB3 are found to be in excellent agreement with its X-ray structure, whereas one residue adopts a different backbone geometry, and two residues are subject to extensive chi1 rotamer averaging. The abundance of dipolar couplings can also yield stereospecific assignments of the non-equivalent methylene protons. For the RNA oligomer, dipolar data yielded stereospecific assignments for six out of the eight C5'H2 groups in the loop region of the oligomer, in all cases confirmed by 1J(C5'H5')>1J(C5'H5"), and H5' resonating downfield of H5".
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