title: Simplification of protein NOESY spectra using bioorganic precursor synthesis and NMR spectral editing.
abstract: 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.affiliation: Institute of Organical Chemistry, Währingerstrasse 38, A-1090 Vienna, Austria.
authors.forename: Roman
authors.initials: R
authors.lastname: Lichtenecker
authors.forename: Martin L
authors.initials: ML
authors.lastname: Ludwiczek
authors.forename: Walther
authors.initials: W
authors.lastname: Schmid
authors.forename: Robert
authors.initials: R
authors.lastname: Konrat
mesh_terms: D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry*
chemical_list: D011506:Proteins