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Solid-State NMR Structure of Microcrystalline UbiquitinSolid-State NMR Structure of Microcrystalline Ubiquitin
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProton-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 AlsoReferences
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