Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets

T. Szyperski; P. Güntert; G. Otting; K. Wüthrich

doi:10.1016/0022-2364(92)90209-P

Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets

T. Szyperski^*, P. Güntert, G. Otting, K. Wüthrich

^*Corresponding author for this work

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

192 Citations (Scopus)

Abstract

A generally applicable new method for the determination of scalar coupling constants for spins with a single coupling partner, in particular ³J_HNα. in polypeptides, is described. It has the special advantage for use in protein structure determinations that no extra NMR experiments need to be recorded, and that NOE distance constraints and dihedral angle constraints from ³J_HNα can be derived from the same data sets. The scalar coupling constants are extracted from the in-phase multiplets of homonuclear [¹H, ¹H] NOESY spectra or heteronuclear [¹⁵N, ¹H ] COSY spectra through inverse Fourier transformation of the data points representing a cross peak along ω₂, and a subsequent nonlinear least-squares fit in the time domain. Practical applications are described for recombinant hirudin and the basic pancreatic trypsin inhibitor.

Original language	English
Pages (from-to)	552-560
Number of pages	9
Journal	Journal of Magnetic Resonance (1969)
Volume	99
Issue number	3
DOIs	https://doi.org/10.1016/0022-2364(92)90209-P
Publication status	Published - 1 Oct 1992
Externally published	Yes

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title = "Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets",

abstract = "A generally applicable new method for the determination of scalar coupling constants for spins with a single coupling partner, in particular 3JHNα. in polypeptides, is described. It has the special advantage for use in protein structure determinations that no extra NMR experiments need to be recorded, and that NOE distance constraints and dihedral angle constraints from 3JHNα can be derived from the same data sets. The scalar coupling constants are extracted from the in-phase multiplets of homonuclear [1H, 1H] NOESY spectra or heteronuclear [15N, 1H ] COSY spectra through inverse Fourier transformation of the data points representing a cross peak along ω2, and a subsequent nonlinear least-squares fit in the time domain. Practical applications are described for recombinant hirudin and the basic pancreatic trypsin inhibitor.",

author = "T. Szyperski and P. G{\"u}ntert and G. Otting and K. W{\"u}thrich",

year = "1992",

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doi = "10.1016/0022-2364(92)90209-P",

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TY - JOUR

T1 - Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets

AU - Szyperski, T.

AU - Güntert, P.

AU - Otting, G.

AU - Wüthrich, K.

PY - 1992/10/1

Y1 - 1992/10/1

N2 - A generally applicable new method for the determination of scalar coupling constants for spins with a single coupling partner, in particular 3JHNα. in polypeptides, is described. It has the special advantage for use in protein structure determinations that no extra NMR experiments need to be recorded, and that NOE distance constraints and dihedral angle constraints from 3JHNα can be derived from the same data sets. The scalar coupling constants are extracted from the in-phase multiplets of homonuclear [1H, 1H] NOESY spectra or heteronuclear [15N, 1H ] COSY spectra through inverse Fourier transformation of the data points representing a cross peak along ω2, and a subsequent nonlinear least-squares fit in the time domain. Practical applications are described for recombinant hirudin and the basic pancreatic trypsin inhibitor.

AB - A generally applicable new method for the determination of scalar coupling constants for spins with a single coupling partner, in particular 3JHNα. in polypeptides, is described. It has the special advantage for use in protein structure determinations that no extra NMR experiments need to be recorded, and that NOE distance constraints and dihedral angle constraints from 3JHNα can be derived from the same data sets. The scalar coupling constants are extracted from the in-phase multiplets of homonuclear [1H, 1H] NOESY spectra or heteronuclear [15N, 1H ] COSY spectra through inverse Fourier transformation of the data points representing a cross peak along ω2, and a subsequent nonlinear least-squares fit in the time domain. Practical applications are described for recombinant hirudin and the basic pancreatic trypsin inhibitor.

UR - https://www.scopus.com/pages/publications/44049114111

U2 - 10.1016/0022-2364(92)90209-P

DO - 10.1016/0022-2364(92)90209-P

M3 - Article

AN - SCOPUS:44049114111

SN - 0022-2364

VL - 99

SP - 552

EP - 560

JO - Journal of Magnetic Resonance (1969)

JF - Journal of Magnetic Resonance (1969)

IS - 3

ER -

Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets

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