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Efficient acquisition of high-resolution 4-D diagonal-suppressed methyl-methyl NOESY for large proteins.

Publication ,  Journal Article
Wen, J; Zhou, P; Wu, J
Published in: J Magn Reson
May 2012

The methyl-methyl NOESY experiment plays an important role in determining the global folds of large proteins. Despite the high sensitivity of this experiment, the analysis of methyl-methyl NOEs is frequently hindered by the limited chemical shift dispersion of methyl groups, particularly methyl protons. This makes it difficult to unambiguously assign all of the methyl-methyl NOE crosspeaks using 3-D spectroscopy. The recent development of sparse sampling methods enables highly efficient acquisition of high-resolution 4-D spectra, which provides an excellent solution to resolving the degeneracy of methyl signals. However, many reconstruction algorithms for processing sparsely-sampled NMR data do not provide adequate suppression of aliasing artifacts in the presence of strong NOE diagonal signals. In order to overcome this limitation, we present a 4-D diagonal-suppressed methyl-methyl NOESY experiment specifically optimized for ultrasparse sampling and evaluate it using a deuterated, ILV methyl-protonated sample of the 42 kDa Escherichia coli maltose binding protein (MBP). Suppression of diagonal signals removes the dynamic range barrier of the methyl-methyl NOESY experiment such that residual aliasing artifacts in the CLEAN-reconstructed high-resolution 4-D spectrum can be further reduced. At an ultrasparse sampling rate of less than 1%, we were able to identify and unambiguously assign the vast majority of expected NOE crosspeaks between methyl groups separated by less than 5 Å and to detect very weak NOE crosspeaks from methyl groups that are over 7 Å apart.

Duke Scholars

Published In

J Magn Reson

DOI

EISSN

1096-0856

Publication Date

May 2012

Volume

218

Start / End Page

128 / 132

Location

United States

Related Subject Headings

  • beta-Cyclodextrins
  • Protons
  • Proteins
  • Methylation
  • Maltose-Binding Proteins
  • Magnetic Resonance Spectroscopy
  • Indicators and Reagents
  • Escherichia coli
  • Biophysics
  • Artifacts
 

Citation

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ICMJE
MLA
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Wen, J., Zhou, P., & Wu, J. (2012). Efficient acquisition of high-resolution 4-D diagonal-suppressed methyl-methyl NOESY for large proteins. J Magn Reson, 218, 128–132. https://doi.org/10.1016/j.jmr.2012.02.021
Wen, Jie, Pei Zhou, and Jihui Wu. “Efficient acquisition of high-resolution 4-D diagonal-suppressed methyl-methyl NOESY for large proteins.J Magn Reson 218 (May 2012): 128–32. https://doi.org/10.1016/j.jmr.2012.02.021.
Wen, Jie, et al. “Efficient acquisition of high-resolution 4-D diagonal-suppressed methyl-methyl NOESY for large proteins.J Magn Reson, vol. 218, May 2012, pp. 128–32. Pubmed, doi:10.1016/j.jmr.2012.02.021.
Journal cover image

Published In

J Magn Reson

DOI

EISSN

1096-0856

Publication Date

May 2012

Volume

218

Start / End Page

128 / 132

Location

United States

Related Subject Headings

  • beta-Cyclodextrins
  • Protons
  • Proteins
  • Methylation
  • Maltose-Binding Proteins
  • Magnetic Resonance Spectroscopy
  • Indicators and Reagents
  • Escherichia coli
  • Biophysics
  • Artifacts