A set of HNCO-based experiments for measurement of residual dipolar couplings in 15N, 13C, (2H)-labeled proteins

P. Permi, P. Rosevear, Arto Annila

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Abstract

Several HNCO-based three-dimensional experiments are described for the measurement of 13C′(i−1)-13Cα(i−1), 15N(i)-13C′(i−1), 15N(i)-13Cα(i), 15N(i)-13Cα(i−1), 1HN(i)-13Cα(i), 1HN(i)-13Cα(i−1), and 13Cα(i−1)-13Cβ(i−1) scalar and dipolar couplings in 15N, 13C, (2H)-labelled protein samples. These pulse sequences produce spin-state edited spectra superficially resembling an HNCO correlation spectrum, allowing accurate and simple measurement of couplings without introducing additional spectral crowding. Scalar and dipolar couplings are measured with good sensitivity from relatively large proteins, as demonstrated with three proteins: cardiac Troponin C, calerythrin and ubiquitin. Measurement of several dipolar couplings between spin-1/2 nuclei using spin-state selective 3D HNCO spectra provides a wealth of structural information.

Original languageEnglish
Pages (from-to)43 - 54
Number of pages12
JournalJournal of Biomolecular NMR
Volume17
Issue number1
DOIs
Publication statusPublished - 2000
MoE publication typeA1 Journal article-refereed

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title = "A set of HNCO-based experiments for measurement of residual dipolar couplings in 15N, 13C, (2H)-labeled proteins",
abstract = "Several HNCO-based three-dimensional experiments are described for the measurement of 13C′(i−1)-13Cα(i−1), 15N(i)-13C′(i−1), 15N(i)-13Cα(i), 15N(i)-13Cα(i−1), 1HN(i)-13Cα(i), 1HN(i)-13Cα(i−1), and 13Cα(i−1)-13Cβ(i−1) scalar and dipolar couplings in 15N, 13C, (2H)-labelled protein samples. These pulse sequences produce spin-state edited spectra superficially resembling an HNCO correlation spectrum, allowing accurate and simple measurement of couplings without introducing additional spectral crowding. Scalar and dipolar couplings are measured with good sensitivity from relatively large proteins, as demonstrated with three proteins: cardiac Troponin C, calerythrin and ubiquitin. Measurement of several dipolar couplings between spin-1/2 nuclei using spin-state selective 3D HNCO spectra provides a wealth of structural information.",
author = "P. Permi and P. Rosevear and Arto Annila",
year = "2000",
doi = "10.1023/A:1008372624615",
language = "English",
volume = "17",
pages = "43 -- 54",
journal = "Journal of Biomolecular NMR",
issn = "0925-2738",
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A set of HNCO-based experiments for measurement of residual dipolar couplings in 15N, 13C, (2H)-labeled proteins. / Permi, P.; Rosevear, P.; Annila, Arto.

In: Journal of Biomolecular NMR, Vol. 17, No. 1, 2000, p. 43 - 54.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - A set of HNCO-based experiments for measurement of residual dipolar couplings in 15N, 13C, (2H)-labeled proteins

AU - Permi, P.

AU - Rosevear, P.

AU - Annila, Arto

PY - 2000

Y1 - 2000

N2 - Several HNCO-based three-dimensional experiments are described for the measurement of 13C′(i−1)-13Cα(i−1), 15N(i)-13C′(i−1), 15N(i)-13Cα(i), 15N(i)-13Cα(i−1), 1HN(i)-13Cα(i), 1HN(i)-13Cα(i−1), and 13Cα(i−1)-13Cβ(i−1) scalar and dipolar couplings in 15N, 13C, (2H)-labelled protein samples. These pulse sequences produce spin-state edited spectra superficially resembling an HNCO correlation spectrum, allowing accurate and simple measurement of couplings without introducing additional spectral crowding. Scalar and dipolar couplings are measured with good sensitivity from relatively large proteins, as demonstrated with three proteins: cardiac Troponin C, calerythrin and ubiquitin. Measurement of several dipolar couplings between spin-1/2 nuclei using spin-state selective 3D HNCO spectra provides a wealth of structural information.

AB - Several HNCO-based three-dimensional experiments are described for the measurement of 13C′(i−1)-13Cα(i−1), 15N(i)-13C′(i−1), 15N(i)-13Cα(i), 15N(i)-13Cα(i−1), 1HN(i)-13Cα(i), 1HN(i)-13Cα(i−1), and 13Cα(i−1)-13Cβ(i−1) scalar and dipolar couplings in 15N, 13C, (2H)-labelled protein samples. These pulse sequences produce spin-state edited spectra superficially resembling an HNCO correlation spectrum, allowing accurate and simple measurement of couplings without introducing additional spectral crowding. Scalar and dipolar couplings are measured with good sensitivity from relatively large proteins, as demonstrated with three proteins: cardiac Troponin C, calerythrin and ubiquitin. Measurement of several dipolar couplings between spin-1/2 nuclei using spin-state selective 3D HNCO spectra provides a wealth of structural information.

U2 - 10.1023/A:1008372624615

DO - 10.1023/A:1008372624615

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VL - 17

SP - 43

EP - 54

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

SN - 0925-2738

IS - 1

ER -