Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC for aromatic spin system identification in uniformly 13C-labeled proteins

Oliver Zerbe; Thomas Szyperski; Marcel Ottiger; Kurt Wüthrich

doi:10.1007/BF00203820

Three-dimensional ¹H-TOCSY-relayed ct-[¹³C,¹H]-HMQC for aromatic spin system identification in uniformly ¹³C-labeled proteins

Oliver Zerbe
, Thomas Szyperski
, Marcel Ottiger
, Kurt Wüthrich

Chemistry

Swiss Federal Institute of Technology Zurich

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

45 Scopus citations

Abstract

Three-dimensional ¹H-TOCSY-relayed ct-[¹³C,¹H]-HMQC is a novel experiment for aromatic spin system identification in uniformly ¹³C-labeled proteins, which is implemented so that it correlates the chemical shift of a given aromatic proton with those of the directly attached carbon and all vicinal protons. The ct-HMQC scheme is used both for overlay of the indirect ¹H and ¹³C chemical shift evolution periods and for the generation of ¹H-¹H antiphase magnetization to accelerate the ¹H-TOCSY magnetization transfer at short mixing times. As an illustration, data recorded for the 18 kDa protein cyclophilin A are presented. Since transverse relaxation of ¹³C-¹H zero-quantum and double-quantum coherences is to first order insensitive to ¹³C-¹H heteronuclear dipolar relaxation, the new experiment should work also for proteins with molecular weights above 20 kDa.

Original language	English
Pages (from-to)	99-106
Number of pages	8
Journal	Journal of Biomolecular NMR
Volume	7
Issue number	2
DOIs	https://doi.org/10.1007/BF00203820
State	Published - 1996

Keywords

C-labeled proteins
Aromatic spin systems
HMQC
Resonance assignments

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10.1007/BF00203820

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title = "Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC for aromatic spin system identification in uniformly 13C-labeled proteins",

abstract = "Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC is a novel experiment for aromatic spin system identification in uniformly 13C-labeled proteins, which is implemented so that it correlates the chemical shift of a given aromatic proton with those of the directly attached carbon and all vicinal protons. The ct-HMQC scheme is used both for overlay of the indirect 1H and 13C chemical shift evolution periods and for the generation of 1H-1H antiphase magnetization to accelerate the 1H-TOCSY magnetization transfer at short mixing times. As an illustration, data recorded for the 18 kDa protein cyclophilin A are presented. Since transverse relaxation of 13C-1H zero-quantum and double-quantum coherences is to first order insensitive to 13C-1H heteronuclear dipolar relaxation, the new experiment should work also for proteins with molecular weights above 20 kDa.",

keywords = "C-labeled proteins, Aromatic spin systems, HMQC, Resonance assignments",

author = "Oliver Zerbe and Thomas Szyperski and Marcel Ottiger and Kurt W{\"u}thrich",

year = "1996",

doi = "10.1007/BF00203820",

language = "English",

volume = "7",

pages = "99--106",

journal = "Journal of Biomolecular NMR",

issn = "0925-2738",

publisher = "Springer Science and Business Media B.V.",

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TY - JOUR

T1 - Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC for aromatic spin system identification in uniformly 13C-labeled proteins

AU - Zerbe, Oliver

AU - Szyperski, Thomas

AU - Ottiger, Marcel

AU - Wüthrich, Kurt

PY - 1996

Y1 - 1996

N2 - Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC is a novel experiment for aromatic spin system identification in uniformly 13C-labeled proteins, which is implemented so that it correlates the chemical shift of a given aromatic proton with those of the directly attached carbon and all vicinal protons. The ct-HMQC scheme is used both for overlay of the indirect 1H and 13C chemical shift evolution periods and for the generation of 1H-1H antiphase magnetization to accelerate the 1H-TOCSY magnetization transfer at short mixing times. As an illustration, data recorded for the 18 kDa protein cyclophilin A are presented. Since transverse relaxation of 13C-1H zero-quantum and double-quantum coherences is to first order insensitive to 13C-1H heteronuclear dipolar relaxation, the new experiment should work also for proteins with molecular weights above 20 kDa.

AB - Three-dimensional 1H-TOCSY-relayed ct-[13C,1H]-HMQC is a novel experiment for aromatic spin system identification in uniformly 13C-labeled proteins, which is implemented so that it correlates the chemical shift of a given aromatic proton with those of the directly attached carbon and all vicinal protons. The ct-HMQC scheme is used both for overlay of the indirect 1H and 13C chemical shift evolution periods and for the generation of 1H-1H antiphase magnetization to accelerate the 1H-TOCSY magnetization transfer at short mixing times. As an illustration, data recorded for the 18 kDa protein cyclophilin A are presented. Since transverse relaxation of 13C-1H zero-quantum and double-quantum coherences is to first order insensitive to 13C-1H heteronuclear dipolar relaxation, the new experiment should work also for proteins with molecular weights above 20 kDa.

KW - C-labeled proteins

KW - Aromatic spin systems

KW - HMQC

KW - Resonance assignments

UR - https://www.scopus.com/pages/publications/0002748328

U2 - 10.1007/BF00203820

DO - 10.1007/BF00203820

M3 - Article

AN - SCOPUS:0002748328

SN - 0925-2738

VL - 7

SP - 99

EP - 106

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

IS - 2

ER -

Three-dimensional ¹H-TOCSY-relayed ct-[¹³C,¹H]-HMQC for aromatic spin system identification in uniformly ¹³C-labeled proteins

Abstract

Keywords

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