3D 13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double-labeled proteins

Thomas Szyperski; Gerhard Wider; John H. Bushweller; Kurt Wüthrich

doi:10.1007/BF00242481

3D ¹³C-¹⁵N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in ¹³C-¹⁵N-double-labeled proteins

Thomas Szyperski
, Gerhard Wider
, John H. Bushweller
, Kurt Wüthrich

Chemistry

University at Buffalo

Swiss Federal Institute of Technology Zurich

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

77 Scopus citations

Abstract

The pulse sequence of a new constant-time 3D triple-resonance experiment, ct-HA[CAN]HN, is presented. This experiment delineates exclusively scalar connectivities and uses ¹³C^α-¹⁵N heteronuclear two-spin coherence to overlay the chemical shift evolution periods of the ¹³C^α and ¹⁵N nuclei, thereby providing the four resonance frequencies of the α-proton, the α-carbon, the amide nitrogen, and the amide proton of a given amino acid residue in three dimensions. This experiment promises to be a valid alternative to 4D experiments, providing the same information on intraresidue polypeptide backbone connectivities in ¹³C-¹⁵N-double-labeled proteins.

Original language	English
Pages (from-to)	127-132
Number of pages	6
Journal	Journal of Biomolecular NMR
Volume	3
Issue number	1
DOIs	https://doi.org/10.1007/BF00242481
State	Published - Jan 1993

Keywords

Heteronuclear two-spin coherence spectroscopy
NMR
Protein structure determination
Resonance assignments

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10.1007/BF00242481

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title = "3D 13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double-labeled proteins",

abstract = "The pulse sequence of a new constant-time 3D triple-resonance experiment, ct-HA[CAN]HN, is presented. This experiment delineates exclusively scalar connectivities and uses 13Cα-15N heteronuclear two-spin coherence to overlay the chemical shift evolution periods of the 13Cα and 15N nuclei, thereby providing the four resonance frequencies of the α-proton, the α-carbon, the amide nitrogen, and the amide proton of a given amino acid residue in three dimensions. This experiment promises to be a valid alternative to 4D experiments, providing the same information on intraresidue polypeptide backbone connectivities in 13C-15N-double-labeled proteins.",

keywords = "Heteronuclear two-spin coherence spectroscopy, NMR, Protein structure determination, Resonance assignments",

author = "Thomas Szyperski and Gerhard Wider and Bushweller, \{John H.\} and Kurt W{\"u}thrich",

year = "1993",

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doi = "10.1007/BF00242481",

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AU - Wider, Gerhard

AU - Bushweller, John H.

AU - Wüthrich, Kurt

PY - 1993/1

Y1 - 1993/1

N2 - The pulse sequence of a new constant-time 3D triple-resonance experiment, ct-HA[CAN]HN, is presented. This experiment delineates exclusively scalar connectivities and uses 13Cα-15N heteronuclear two-spin coherence to overlay the chemical shift evolution periods of the 13Cα and 15N nuclei, thereby providing the four resonance frequencies of the α-proton, the α-carbon, the amide nitrogen, and the amide proton of a given amino acid residue in three dimensions. This experiment promises to be a valid alternative to 4D experiments, providing the same information on intraresidue polypeptide backbone connectivities in 13C-15N-double-labeled proteins.

AB - The pulse sequence of a new constant-time 3D triple-resonance experiment, ct-HA[CAN]HN, is presented. This experiment delineates exclusively scalar connectivities and uses 13Cα-15N heteronuclear two-spin coherence to overlay the chemical shift evolution periods of the 13Cα and 15N nuclei, thereby providing the four resonance frequencies of the α-proton, the α-carbon, the amide nitrogen, and the amide proton of a given amino acid residue in three dimensions. This experiment promises to be a valid alternative to 4D experiments, providing the same information on intraresidue polypeptide backbone connectivities in 13C-15N-double-labeled proteins.

KW - Heteronuclear two-spin coherence spectroscopy

KW - NMR

KW - Protein structure determination

KW - Resonance assignments

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JF - Journal of Biomolecular NMR

IS - 1

ER -

3D ¹³C-¹⁵N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in ¹³C-¹⁵N-double-labeled proteins

Abstract

Keywords

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