Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the α-subunit of human chorionic gonadotropin

T. De Beer; C.W.E.M. Van Zuylen; K. Hard; R. Boelens; R. Kaptein; J.P. Kamerling; J.F.G. Vliegenthart

doi:10.1016/0014-5793(94)00547-8

Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the α-subunit of human chorionic gonadotropin

T. De Beer, C.W.E.M. Van Zuylen, K. Hard, R. Boelens, R. Kaptein, J.P. Kamerling, J.F.G. Vliegenthart

Sub NMR Spectroscopy

Bijvoet Center

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

Abstract

The structure assessment of an intact glycoprotein in solution requires an extensive assignment of the carbohydrate NMR resonances. However, assignment of homonuclear spectra is very complicated because of the severe overlap of protein and carbohydrate signals. Application of pulsed field gradients allowed high quality natural abundance 1H-13C HSQC and HSQC-TOCSY spectra to be recorded of the α-subunit of human chorionic gonadotropin. Most carbohydrate 1H-13C correlations appear in a distinct region between the aromatic region and the protein C(α)H(α) region. The enormous reduction in overlap led to fast and unambiguous assignment of the anomeric 1H-13C correlations. Subsequently, correlations of the monosaccharide skeleton atoms were readily assigned in the HSQC-TOCSY spectrum.

Original language	English
Pages (from-to)	1-6
Number of pages	6
Journal	FEBS Letters
Volume	348
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(94)00547-8
Publication status	Published - 9 Jul 1994

Keywords

α-subunit
1H-13C correlation spectroscopy
Glycoprotein
Human chorionic gonadotropin
Nuclear magnetic resonance
Pulsed field gradients
carbohydrate
chorionic gonadotropin
glycoprotein
article
chemical structure
nuclear magnetic resonance
priority journal

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De Beer, T., Van Zuylen, C. W. E. M., Hard, K., Boelens, R., Kaptein, R., Kamerling, J. P., & Vliegenthart, J. F. G. (1994). Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the α-subunit of human chorionic gonadotropin. FEBS Letters, 348(1), 1-6. https://doi.org/10.1016/0014-5793(94)00547-8

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title = "Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the α-subunit of human chorionic gonadotropin",

abstract = "The structure assessment of an intact glycoprotein in solution requires an extensive assignment of the carbohydrate NMR resonances. However, assignment of homonuclear spectra is very complicated because of the severe overlap of protein and carbohydrate signals. Application of pulsed field gradients allowed high quality natural abundance 1H-13C HSQC and HSQC-TOCSY spectra to be recorded of the α-subunit of human chorionic gonadotropin. Most carbohydrate 1H-13C correlations appear in a distinct region between the aromatic region and the protein C(α)H(α) region. The enormous reduction in overlap led to fast and unambiguous assignment of the anomeric 1H-13C correlations. Subsequently, correlations of the monosaccharide skeleton atoms were readily assigned in the HSQC-TOCSY spectrum.",

keywords = "α-subunit, 1H-13C correlation spectroscopy, Glycoprotein, Human chorionic gonadotropin, Nuclear magnetic resonance, Pulsed field gradients, carbohydrate, chorionic gonadotropin, glycoprotein, article, chemical structure, nuclear magnetic resonance, priority journal",

author = "{De Beer}, T. and {Van Zuylen}, C.W.E.M. and K. Hard and R. Boelens and R. Kaptein and J.P. Kamerling and J.F.G. Vliegenthart",

year = "1994",

month = jul,

day = "9",

doi = "10.1016/0014-5793(94)00547-8",

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De Beer, T, Van Zuylen, CWEM, Hard, K, Boelens, R , Kaptein, R , Kamerling, JP & Vliegenthart, JFG 1994, 'Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the α-subunit of human chorionic gonadotropin', FEBS Letters, vol. 348, no. 1, pp. 1-6. https://doi.org/10.1016/0014-5793(94)00547-8

Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the α-subunit of human chorionic gonadotropin. / De Beer, T.; Van Zuylen, C.W.E.M.; Hard, K. et al.
In: FEBS Letters, Vol. 348, No. 1, 09.07.1994, p. 1-6.

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

TY - JOUR

T1 - Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the α-subunit of human chorionic gonadotropin

AU - De Beer, T.

AU - Van Zuylen, C.W.E.M.

AU - Hard, K.

AU - Boelens, R.

AU - Kaptein, R.

AU - Kamerling, J.P.

AU - Vliegenthart, J.F.G.

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N2 - The structure assessment of an intact glycoprotein in solution requires an extensive assignment of the carbohydrate NMR resonances. However, assignment of homonuclear spectra is very complicated because of the severe overlap of protein and carbohydrate signals. Application of pulsed field gradients allowed high quality natural abundance 1H-13C HSQC and HSQC-TOCSY spectra to be recorded of the α-subunit of human chorionic gonadotropin. Most carbohydrate 1H-13C correlations appear in a distinct region between the aromatic region and the protein C(α)H(α) region. The enormous reduction in overlap led to fast and unambiguous assignment of the anomeric 1H-13C correlations. Subsequently, correlations of the monosaccharide skeleton atoms were readily assigned in the HSQC-TOCSY spectrum.

AB - The structure assessment of an intact glycoprotein in solution requires an extensive assignment of the carbohydrate NMR resonances. However, assignment of homonuclear spectra is very complicated because of the severe overlap of protein and carbohydrate signals. Application of pulsed field gradients allowed high quality natural abundance 1H-13C HSQC and HSQC-TOCSY spectra to be recorded of the α-subunit of human chorionic gonadotropin. Most carbohydrate 1H-13C correlations appear in a distinct region between the aromatic region and the protein C(α)H(α) region. The enormous reduction in overlap led to fast and unambiguous assignment of the anomeric 1H-13C correlations. Subsequently, correlations of the monosaccharide skeleton atoms were readily assigned in the HSQC-TOCSY spectrum.

KW - α-subunit

KW - 1H-13C correlation spectroscopy

KW - Glycoprotein

KW - Human chorionic gonadotropin

KW - Nuclear magnetic resonance

KW - Pulsed field gradients

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KW - glycoprotein

KW - article

KW - chemical structure

KW - nuclear magnetic resonance

KW - priority journal

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JO - FEBS Letters

JF - FEBS Letters

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De Beer T, Van Zuylen CWEM, Hard K, Boelens R , Kaptein R , Kamerling JP et al. Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the α-subunit of human chorionic gonadotropin. FEBS Letters. 1994 Jul 9;348(1):1-6. doi: 10.1016/0014-5793(94)00547-8