Amino Acid-Type Edited NMR Experiments for Methyl−Methyl Distance Measurement in 13C-Labeled Proteins

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Abstract

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