Amino acid-type edited NMR experiments for methyl-methyl distance measurement in 13C-labeled proteins.
New NMR experiments are presented for the measurement of methyl-methyl distances in (13)C-labeled proteins from a series of amino acid-type separated 2D or 3D NOESY spectra. Hadamard amino acid-type encoding of the proximal methyl groups provides the high spectral resolution required for unambiguous methyl-methyl NOE assignment, which is particularly important for fast global fold determination of proteins. The experiments can be applied to a wide range of protein systems, as exemplified for two small proteins, ubiquitin and MerAa, and the 30 kDa BRP-Blm complex.
Institut de Biologie Structurale, Jean-Pierre Ebel CNRS-CEA-UJF, 41, rue Jules Horowitz, 38027 Grenoble Cedex, France.
Hélène
H
Van Melckebeke
Jean-Pierre
JP
Simorre
Bernhard
B
Brutscher
D000123:Acetyltransferases / Q000737:chemistry*; D000596:Amino Acids / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry*; D001761:Bleomycin / Q000737:chemistry; D002247:Carbon Isotopes; D006801:Humans; D007553:Isotope Labeling; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010088:Oxidoreductases / Q000737:chemistry*; D043367:Ralstonia / Q000201:enzymology; D025801:Ubiquitin / Q000737:chemistry*
D000596:Amino Acids; D001426:Bacterial Proteins; D002247:Carbon Isotopes; D025801:Ubiquitin; D001761:Bleomycin; D010088:Oxidoreductases; C021551:mercuric reductase; C087954:bleomycin N-acetyltransferase; D000123:Acetyltransferases