Abstract
Two methods for the measurement of homonuclear 3JHNHα coupling constants are described. Both HSQC- and HMQC-type experiments employ 'quantitative J-correlation', in which the coupling constant of interest is obtained from the intensity ratio of cross peaks of two spectra. The first spectrum is acquired with 3JHNHα evolution and the second with α-proton decoupling. The resolution of these methods in the F1-domain is not restricted.
Original language | English |
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Pages (from-to) | 29 - 37 |
Number of pages | 9 |
Journal | Journal of Biomolecular NMR |
Volume | 16 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2000 |
MoE publication type | A1 Journal article-refereed |
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Intensity modulated HSQC and HMQC : Two simple methods to measure 3JHNHα in proteins. / Permi, P.; Kilpeläinen, I.; Annila, Arto; Heikkinen, S. (Corresponding Author).
In: Journal of Biomolecular NMR, Vol. 16, No. 1, 2000, p. 29 - 37.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Intensity modulated HSQC and HMQC
T2 - Two simple methods to measure 3JHNHα in proteins
AU - Permi, P.
AU - Kilpeläinen, I.
AU - Annila, Arto
AU - Heikkinen, S.
PY - 2000
Y1 - 2000
N2 - Two methods for the measurement of homonuclear 3JHNHα coupling constants are described. Both HSQC- and HMQC-type experiments employ 'quantitative J-correlation', in which the coupling constant of interest is obtained from the intensity ratio of cross peaks of two spectra. The first spectrum is acquired with 3JHNHα evolution and the second with α-proton decoupling. The resolution of these methods in the F1-domain is not restricted.
AB - Two methods for the measurement of homonuclear 3JHNHα coupling constants are described. Both HSQC- and HMQC-type experiments employ 'quantitative J-correlation', in which the coupling constant of interest is obtained from the intensity ratio of cross peaks of two spectra. The first spectrum is acquired with 3JHNHα evolution and the second with α-proton decoupling. The resolution of these methods in the F1-domain is not restricted.
U2 - 10.1023/A:1008343926502
DO - 10.1023/A:1008343926502
M3 - Article
VL - 16
SP - 29
EP - 37
JO - Journal of Biomolecular NMR
JF - Journal of Biomolecular NMR
SN - 0925-2738
IS - 1
ER -