TY - JOUR
T1 - Zooming, a practical strategy for improving the quality of multidimensional NMR spectra
AU - Zolnai, Zsolt
AU - Juranić, Nenad
AU - Markley, John L.
AU - Macura, Slobodan
N1 - Funding Information:
Zs.Z. and J.L.M. were supported by Grant RR 02301 from the Biomedical Research Technology Program, National Center for Research Resources, National Institutes of Health.
PY - 1996
Y1 - 1996
N2 - A method has been developed, which is termed "zooming," that provides high digital resolution in any region selected from an n-dimensional data set. The region selected can be of arbitrary size (any number of data points). In the zooming approach as implemented in the "ZOOM" computer program, the desired region of the frequency-domain spectrum is first extracted. Next, a "pseudo-FID" for the selected region is constructed by n-dimensional inverse Fourier transformation. The resulting time-domain data block is zero filled in n -dimensions and finally Fourier transformed back to the frequency domain. The basic principles behind the zooming approach are described, and its application to the analysis of 2D and 3D NMR data from proteins is demonstrated. Zooming is expected to be of even greater importance in the analysis of higher-dimensional NMR data where problems of acquisition and processing times and data storage space become more pronounced. The implementation described here is for spectra consisting of real or absolute-value data; at least one zero fill must have been applied in each dimension during the initial processing of the data.
AB - A method has been developed, which is termed "zooming," that provides high digital resolution in any region selected from an n-dimensional data set. The region selected can be of arbitrary size (any number of data points). In the zooming approach as implemented in the "ZOOM" computer program, the desired region of the frequency-domain spectrum is first extracted. Next, a "pseudo-FID" for the selected region is constructed by n-dimensional inverse Fourier transformation. The resulting time-domain data block is zero filled in n -dimensions and finally Fourier transformed back to the frequency domain. The basic principles behind the zooming approach are described, and its application to the analysis of 2D and 3D NMR data from proteins is demonstrated. Zooming is expected to be of even greater importance in the analysis of higher-dimensional NMR data where problems of acquisition and processing times and data storage space become more pronounced. The implementation described here is for spectra consisting of real or absolute-value data; at least one zero fill must have been applied in each dimension during the initial processing of the data.
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U2 - 10.1006/jmra.1996.0051
DO - 10.1006/jmra.1996.0051
M3 - Article
AN - SCOPUS:0001982927
SN - 1064-1858
VL - 119
SP - 53
EP - 64
JO - Journal of Magnetic Resonance - Series A
JF - Journal of Magnetic Resonance - Series A
IS - 1
ER -