Fast (4,3)D GFT-TS NMR for NOESY of small to medium-sized proteins

Youlin Xia; Sudha Veeraraghavan; Qi Zhu; Xiaolian Gao

doi:10.1016/j.jmr.2007.09.015

Fast (4,3)D GFT-TS NMR for NOESY of small to medium-sized proteins

Youlin Xia, Sudha Veeraraghavan, Qi Zhu, Xiaolian Gao

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

NOESY NMR spectra provide interproton distance information for a molecule in solution and the complete, unambiguous determination of NOESY spectral assignments is the basis for protein structure determination. High resolution NOESY can be obtained from ¹³C and ¹⁵N isotope edited four-dimensional (4D) data, but these experiments would normally require weeks to complete. We have applied a G-matrix Fourier transform and time-sharing (GFT-TS) NMR method for simultaneously acquiring two sets of 4D NOESY data. The implementation of the GFT-TS allows 2.5- to 5-fold reduction in experimental time without sacrificing spectral resolution as compared with that of 3D data. The ¹³C, ¹⁵N-edited GFT-TS (4,3)D H-N-CN-H NOESY (GFT dimensions are underlined and TS dimensions are in italics) provides convenient and unambiguous NOE assignments for HN/HN and HN/HC for a sample of 1.4 mM ubiquitin (76 amino acids, 8.5 kDa). We also provide a set of utility scripts for data processing and spectral assignment to facilitate the use of GFT NMR. This method shows great promise for routine high quality NMR NOESY data collection for small to medium sized proteins.

Original language	English (US)
Pages (from-to)	142-148
Number of pages	7
Journal	Journal of Magnetic Resonance
Volume	190
Issue number	1
DOIs	https://doi.org/10.1016/j.jmr.2007.09.015
State	Published - Jan 2008
Externally published	Yes

Bibliographical note

Funding Information:
The 800 MHz NMR spectrometer at the Keck/IMD NMR Center at the University of Houston is funded by the W. M. Keck Foundation and the University of Houston. This research was in part supported by grants from NIH (R42 GM067364) and the Robert A. Welch Foundation (E-1027).

Keywords

GFT NMR
NOESY
RD NMR
Time-sharing (TS)

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title = "Fast (4,3)D GFT-TS NMR for NOESY of small to medium-sized proteins",

abstract = "NOESY NMR spectra provide interproton distance information for a molecule in solution and the complete, unambiguous determination of NOESY spectral assignments is the basis for protein structure determination. High resolution NOESY can be obtained from 13C and 15N isotope edited four-dimensional (4D) data, but these experiments would normally require weeks to complete. We have applied a G-matrix Fourier transform and time-sharing (GFT-TS) NMR method for simultaneously acquiring two sets of 4D NOESY data. The implementation of the GFT-TS allows 2.5- to 5-fold reduction in experimental time without sacrificing spectral resolution as compared with that of 3D data. The 13C, 15N-edited GFT-TS (4,3)D H-N-CN-H NOESY (GFT dimensions are underlined and TS dimensions are in italics) provides convenient and unambiguous NOE assignments for HN/HN and HN/HC for a sample of 1.4 mM ubiquitin (76 amino acids, 8.5 kDa). We also provide a set of utility scripts for data processing and spectral assignment to facilitate the use of GFT NMR. This method shows great promise for routine high quality NMR NOESY data collection for small to medium sized proteins.",

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note = "Funding Information: The 800 MHz NMR spectrometer at the Keck/IMD NMR Center at the University of Houston is funded by the W. M. Keck Foundation and the University of Houston. This research was in part supported by grants from NIH (R42 GM067364) and the Robert A. Welch Foundation (E-1027). ",

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AU - Zhu, Qi

AU - Gao, Xiaolian

N1 - Funding Information: The 800 MHz NMR spectrometer at the Keck/IMD NMR Center at the University of Houston is funded by the W. M. Keck Foundation and the University of Houston. This research was in part supported by grants from NIH (R42 GM067364) and the Robert A. Welch Foundation (E-1027).

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N2 - NOESY NMR spectra provide interproton distance information for a molecule in solution and the complete, unambiguous determination of NOESY spectral assignments is the basis for protein structure determination. High resolution NOESY can be obtained from 13C and 15N isotope edited four-dimensional (4D) data, but these experiments would normally require weeks to complete. We have applied a G-matrix Fourier transform and time-sharing (GFT-TS) NMR method for simultaneously acquiring two sets of 4D NOESY data. The implementation of the GFT-TS allows 2.5- to 5-fold reduction in experimental time without sacrificing spectral resolution as compared with that of 3D data. The 13C, 15N-edited GFT-TS (4,3)D H-N-CN-H NOESY (GFT dimensions are underlined and TS dimensions are in italics) provides convenient and unambiguous NOE assignments for HN/HN and HN/HC for a sample of 1.4 mM ubiquitin (76 amino acids, 8.5 kDa). We also provide a set of utility scripts for data processing and spectral assignment to facilitate the use of GFT NMR. This method shows great promise for routine high quality NMR NOESY data collection for small to medium sized proteins.

AB - NOESY NMR spectra provide interproton distance information for a molecule in solution and the complete, unambiguous determination of NOESY spectral assignments is the basis for protein structure determination. High resolution NOESY can be obtained from 13C and 15N isotope edited four-dimensional (4D) data, but these experiments would normally require weeks to complete. We have applied a G-matrix Fourier transform and time-sharing (GFT-TS) NMR method for simultaneously acquiring two sets of 4D NOESY data. The implementation of the GFT-TS allows 2.5- to 5-fold reduction in experimental time without sacrificing spectral resolution as compared with that of 3D data. The 13C, 15N-edited GFT-TS (4,3)D H-N-CN-H NOESY (GFT dimensions are underlined and TS dimensions are in italics) provides convenient and unambiguous NOE assignments for HN/HN and HN/HC for a sample of 1.4 mM ubiquitin (76 amino acids, 8.5 kDa). We also provide a set of utility scripts for data processing and spectral assignment to facilitate the use of GFT NMR. This method shows great promise for routine high quality NMR NOESY data collection for small to medium sized proteins.

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Fast (4,3)D GFT-TS NMR for NOESY of small to medium-sized proteins

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