4.8 Article

Amino acid-type edited NMR experiments for methyl-methyl distance measurement in 13C-labeled proteins

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 126, Issue 31, Pages 9584-9591

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja0489644

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New NMR experiments are presented for the measurement of methyl-methyl distances in C-13-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.

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