| Simplification of protein NOESY spectra using bioorganic precursor synthesis and NMR spectral editing. | |
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MedLine Citation:
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PMID: 15113192 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A novel method is proposed for the analysis of protein NOEs in solution. In this approach, chemically synthesized precursor compounds for the amino acids valine, leucine, and isoleucine are used for amino acid specific labeling of these hydrophobic residues. The methodology is based on a novel synthetic route to 12C,1H,2H Val, Leu, and Ile side chains selectively labeled with 13CH3 only at the terminal methyl group. In an otherwise 12C,1H labeled protein, discrimination between protons bound to 12C and 13C (or 15N) can be achieved using standard isotope-editing NMR pulse schemes. This strategy significantly relieves problems with spectral overlap through selective observation of interresidue methyl NOEs and will thus be a powerful extension of existing biomolecular NMR methodology. |
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Authors:
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Roman Lichtenecker; Martin L Ludwiczek; Walther Schmid; Robert Konrat |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of the American Chemical Society Volume: 126 ISSN: 0002-7863 ISO Abbreviation: J. Am. Chem. Soc. Publication Date: 2004 May |
Date Detail:
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Created Date: 2004-04-28 Completed Date: 2004-08-16 Revised Date: 2008-01-17 |
Medline Journal Info:
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Nlm Unique ID: 7503056 Medline TA: J Am Chem Soc Country: United States |
Other Details:
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Languages: eng Pagination: 5348-9 Citation Subset: IM |
Affiliation:
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Institute of Organical Chemistry, Währingerstrasse 38, A-1090 Vienna, Austria. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Molecular Structure Nuclear Magnetic Resonance, Biomolecular* Proteins / chemical synthesis*, chemistry* |
| Chemical | |
Reg. No./Substance:
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0/Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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