(4,2)D Projection-Reconstruction Experiments for Protein Backbone Assignment: Application to Human Carbonic Anhydrase II and Calbindin D.
Projection—-reconstruction NMR experiments have been shown to significantly reduce the acquisition time required to obtain protein backbone assignment data. To date, this concept has only been applied to smaller N/C-labeled proteins. Here, we show that projection—reconstruction NMR techniques can be...
| Publicado en: | Journal of the American Chemical Society Vol. 127; no. 24; pp. 8785 - 8796 |
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| Autores principales: | , , , , |
| Formato: | Artículo |
| Publicado: |
American Chemical Society
6/22/2005
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| Materias: | |
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=17496194&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 17496194 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 6/22/2005 vid: 127 iid: 24 pid: 997 pub: American Chemical Society artinfo: ui: 17496194 10.1021/ja0509580 ppf: 8785 ppct: 11 formats: tig: atl: (4,2)D Projection-Reconstruction Experiments for Protein Backbone Assignment: Application to Human Carbonic Anhydrase II and Calbindin D. aug: au: Venters, Ronald A. Coggins, Brian E. Doug Kojetin Cavanagh, John Pei Zhou affil: Duke University NMR Center, North Carolina 27710, Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710. Duke University Medical Center, Durham, North Carolina 27710, Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710. Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695. su: Carbonic anhydrase Zinc enzymes Biomolecules Resonance Proteins Organic compounds sug: subj: Carbonic anhydrase Zinc enzymes Biomolecules Resonance Proteins Organic compounds ab: Projection—-reconstruction NMR experiments have been shown to significantly reduce the acquisition time required to obtain protein backbone assignment data. To date, this concept has only been applied to smaller N/C-labeled proteins. Here, we show that projection—reconstruction NMR techniques can be extended to larger protonated and perdeuterated proteins. We present a suite of (4,2)D triple-resonance experiments for protein backbone assignment and a Hybrid Backprojection/Lower-Value algorithm for reconstructing data with relatively weak signal-to-noise ratios. In addition, we propose a sampling theorem and discuss its implication on the choice of projection angles. We demonstrate the efficacy of this approach using the 29 kDa protein, human carbonic anhydrase II and the 30 kDa protein, calbindin D. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2005 holdings: @attributes: islocal: N |
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