ArticleJournal of biomolecular NMR2004
Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning.
Article in Journal of biomolecular NMR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Direct assignment ofJournal of biomolecular NMR · 2018Article
- Active-site structure of the thermophilic Foc-subunit ring in membranes elucidated by solid-state NMR.Biophysical journal · 2014Article
- Secondary structural analysis of proteins based on (13)C chemical shift assignments in unresolved solid-state NMR spectra enhanced by fragmented structure database.Journal of biomolecular NMR · 2013Article
- Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.Journal of biomolecular NMR · 2010Article
- Atomic structure of the bacteriochlorophyll c assembly in intact chlorosomes from Chlorobium limicola determined by solid-state NMR.Photosynthesis research · 2010Article
- Solid-state 2H NMR spectroscopy of retinal proteins in aligned membranes.Biochimica et biophysica acta · 2007Review
- ICMRBS founder's medal 2006: biological solid-state NMR, methods and applications.Journal of biomolecular NMR · 2007Article
- Spectral fitting for signal assignment and structural analysis of uniformly 13C-labeled solid proteins by simulated annealing based on chemical shifts and spin dynamics.Journal of biomolecular NMR · 2007Article
- Structure of the light-harvesting bacteriochlorophyll c assembly in chlorosomes from Chlorobium limicola determined by solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Signal assignment and secondary structure analysis of a uniformly [13C, 15N]-labeled membrane protein, H +-ATP synthase subunit c, by magic-angle spinning solid-state NMR.Journal of biomolecular NMR · 2006Article
- Structure of tightly membrane-bound mastoparan-X, a G-protein-activating peptide, determined by solid-state NMR.Biophysical journal · 2006Article
- Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.Journal of biomolecular NMR · 2005Article
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7 authors.
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Abstract
Carbon-13 and nitrogen-15 signals of fully isotope-labeled 15-residue peptide, glycinated mastoparan-X, in a solid state were assigned by two- and three-dimensional NMR experiments under magic-angle spinning conditions. Intra-residue spin connectivities were obtained with multidimensional correlation experiments for C'-C(alpha)-C(beta) and N-C(alpha)-C(beta). Sequence specific assignments were performed with inter-residue C(alpha)-C(alpha) and N-C(alpha)C(beta) correlation experiments. Pulse sequences for these experiments have mixing periods under recoupled zero- and double-quantum (13)C-(13)C and (15)N-(13)C dipolar interactions. These correlation spectra allowed the complete assignments of (13)C and (15)N backbone and (13)C(beta) signals. Chemical shift analysis of the (13)C and (15)N signals based on empirical and quantum chemical databases for proteins indicated that the backbone between residues 3 and 14 forms alpha-helix and residue 2 has extended conformation in the solid state. This structure was compared with the G-protein- and membrane-bound structures of mastoparan-X.
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