Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
Proton-driven 13C spin diffusion (PDSD) is a simple and robust two-dimensional NMR experiment. It leads to spectra with a high signal-to-noise ratio in which cross-peaks contain information about internuclear distances. We show that the total information content is sufficient to determine the atomic-resolution structure of a small protein from a single, uniformly 13C-, 15N-labeled microcrystalline sample. For the example of ubiquitin, the structure was determined by a manual procedure followed by an automatic optimization of the manual structure as well as by a fully automated structure determination approach. The relationship between internuclear distances and cross-peak intensities in the spectra is investigated.
Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy.,Manolikas T, Herrmann T, Meier BH J Am Chem Soc. 2008 Mar 26;130(12):3959-66. Epub 2008 Mar 6. PMID:18321098[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Manolikas T, Herrmann T, Meier BH. Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy. J Am Chem Soc. 2008 Mar 26;130(12):3959-66. Epub 2008 Mar 6. PMID:18321098 doi:10.1021/ja078039s
