ArticlePloS one2008
High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Atomic-Resolution Structure of the Protein Encoded by Gene V of fd Bacteriophage in Complex with Viral ssDNA Determined by Magic-Angle Spinning Solid-State NMR.Journal of the American Chemical Society · 2023Article
- Peptide toxins and small-molecule blockers of BK channels.Acta pharmacologica Sinica · 2016Review
- Scorpion toxins prefer salt solutions.Journal of molecular modeling · 2015Article
- Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy.Nature chemistry · 2012Article
- A Monte Carlo/simulated annealing algorithm for sequential resonance assignment in solid state NMR of uniformly labeled proteins with magic-angle spinning.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2010Article
- High-resolution solid-state NMR structure of a 17.6 kDa protein.Journal of the American Chemical Society · 2010Article
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Paramagnetic shifts in solid-state NMR of proteins to elicit structural information.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.
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