Document Detail


Simplification of protein NOESY spectra using bioorganic precursor synthesis and NMR spectral editing.
MedLine Citation:
PMID:  15113192     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Roman Lichtenecker; Martin L Ludwiczek; Walther Schmid; Robert Konrat
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  126     ISSN:  0002-7863     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2004 May 
Date Detail:
Created Date:  2004-04-28     Completed Date:  2004-08-16     Revised Date:  2008-01-17    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5348-9     Citation Subset:  IM    
Affiliation:
Institute of Organical Chemistry, Währingerstrasse 38, A-1090 Vienna, Austria.
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MeSH Terms
Descriptor/Qualifier:
Molecular Structure
Nuclear Magnetic Resonance, Biomolecular*
Proteins / chemical synthesis*,  chemistry*
Chemical
Reg. No./Substance:
0/Proteins

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