ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2010
3D (13)C-(13)C-(13)C correlation NMR for de novo distance determination of solid proteins and application to a human alpha-defensin.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Polysaccharide assemblies in fungal and plant cell walls explored by solid-state NMR.Structure (London, England : 1993) · 2023Review
- Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism.Nature structural & molecular biology · 2020Article
- Solid-state NMR investigations of cellulose structure and interactions with matrix polysaccharides in plant primary cell walls.Journal of experimental botany · 2016Review
- Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.Solid state nuclear magnetic resonance · 2015Article
- Relaxation-compensated difference spin diffusion NMR for detecting 13C-13C long-range correlations in proteins and polysaccharides.Journal of biomolecular NMR · 2015Article
- Resonance assignment of the NMR spectra of disordered proteins using a multi-objective non-dominated sorting genetic algorithm.Journal of biomolecular NMR · 2013Article
- Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.Protein science : a publication of the Protein Society · 2011Article
- The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption.Biochemistry · 2010Article
- Intramolecular 1H-13C distance measurement in uniformly 13C, 15N labeled peptides by solid-state NMR.Solid state nuclear magnetic resonanceArticle
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3 authors.
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Abstract
The de novo structure of an antimicrobial protein, human alpha-defensin 1 (HNP-1), is determined by combining a 3D (13)C-(13)C-(13)C (CCC) magic-angle spinning (MAS) correlation experiment with standard resonance assignment experiments. Using a short spin diffusion mixing time to assign intra-residue cross peaks and a long mixing time to detect inter-residue correlation peaks, we show that the 3D CCC experiment not only reduces the ambiguity of resonance assignment, but more importantly yields two orders of magnitude more long-range distances without recourse to existing crystal structures. Most of these distance constraints could not be obtained in a de novo fashion from 2D correlation spectra due to significant resonance overlap. Combining the distance constraints from the 3D CCC experiment and the chemical-shift-derived torsion angles, we obtained a de novo high-resolution NMR structure of HNP-1, with a heavy-atom RMSD of 3.4A from the crystal structure of the analogous HNP-3. The average energy of the minimum-energy ensemble is less than of 40kcal/mol. Thus, the 3D CCC experiment provides a reliable means of restraining the three-dimensional structure of insoluble proteins with unknown conformations.
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