Intensity modulated HSQC and HMQC

Two simple methods to measure 3JHNHα in proteins

P. Permi, I. Kilpeläinen, Arto Annila, S. Heikkinen (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

17 Citations (Scopus)

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 languageEnglish
Pages (from-to)29 - 37
Number of pages9
JournalJournal of Biomolecular NMR
Volume16
Issue number1
DOIs
Publication statusPublished - 2000
MoE publication typeA1 Journal article-refereed

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Cite this

Permi, P. ; Kilpeläinen, I. ; Annila, Arto ; Heikkinen, S. / Intensity modulated HSQC and HMQC : Two simple methods to measure 3JHNHα in proteins. In: Journal of Biomolecular NMR. 2000 ; Vol. 16, No. 1. pp. 29 - 37.
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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.",
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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 journalArticleScientificpeer-review

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AU - Permi, P.

AU - Kilpeläinen, I.

AU - Annila, Arto

AU - Heikkinen, S.

PY - 2000

Y1 - 2000

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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.

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