TY - JOUR
T1 - Spline method for correcting baseplane distortions in two-dimensional NMR spectra
AU - Zolnai, Zsolt
AU - Macura, Slobodan
AU - Markley, John L.
N1 - Funding Information:
The authors thank Dr. A. D. Robertson for supplying the protein sample needed in these studies. This research was supported by NIH Grants RR0230 1 and GM35976. The work was carried out at the National Magnetic Resonance Facility at Madison, which is supported in part by NIH Grant RR02301 from the Biomedical Research Technology Program, Division of Research Resources. Equipment in the facility was purchased with funds from the University of Wisconsin, the NSF Biological Instrumentation Program (Grant PCM-84 15048), NIH Biomedical Research Technology Program (RR0203 1)) NIH Shared Instrumentation Program (Grant RR0278 l), and the U.S. Department of Agriculture.
PY - 1989/5
Y1 - 1989/5
N2 - A two-dimensional spline method for correcting baseplane distortions in two-dimensional NMR spectra has been developed. Practical application of the method (selection of the network of reference points, calculation of new values for corrected points, prevention of distortions by diagonal ridges, etc.) is illustrated with two-dimensional cross-relaxation spectra of a small protein (turkey ovomucoid third domain, Mr 6062). Baseplane flattening is particularly important for quantitative analysis of 2D NOE and ROE spectra where baseplane distortion can severely interfere with the measurement of cross-peak volumes; it may also eliminate other artifacts in 2D NMR spectra, such as phase distortion, t1 and t2 ridges, and axial peaks. The procedure significantly improves the visual appearance of 2D spectra and makes them more amenable to automated computer calculation of spectral parameters.
AB - A two-dimensional spline method for correcting baseplane distortions in two-dimensional NMR spectra has been developed. Practical application of the method (selection of the network of reference points, calculation of new values for corrected points, prevention of distortions by diagonal ridges, etc.) is illustrated with two-dimensional cross-relaxation spectra of a small protein (turkey ovomucoid third domain, Mr 6062). Baseplane flattening is particularly important for quantitative analysis of 2D NOE and ROE spectra where baseplane distortion can severely interfere with the measurement of cross-peak volumes; it may also eliminate other artifacts in 2D NMR spectra, such as phase distortion, t1 and t2 ridges, and axial peaks. The procedure significantly improves the visual appearance of 2D spectra and makes them more amenable to automated computer calculation of spectral parameters.
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U2 - 10.1016/0022-2364(89)90213-8
DO - 10.1016/0022-2364(89)90213-8
M3 - Article
AN - SCOPUS:6144270230
SN - 0022-2364
VL - 82
SP - 496
EP - 504
JO - Journal of Magnetic Resonance (1969)
JF - Journal of Magnetic Resonance (1969)
IS - 3
ER -