A new approach for obtaining sequential assignment of large proteins

P. Permi, Arto Annila

Research output: Contribution to journalArticleScientificpeer-review

25 Citations (Scopus)

Abstract

A novel NMR experiment for obtaining sequential assignment of large proteins and protein complexes is described. The proposed method takes full advantage of transverse relaxation optimized spectroscopy (TROSY) and utilizes spin-state-selection to distinguish between intraresidual and sequential connectivities in the HNCA-TROSY-type correlation experiment. Thus, the intra- and interresidual cross peaks can be identified without relaying magnetization via carbonyl carbon, which relaxes very rapidly at the high magnetic fields where TROSY is most efficient. In addition, the presented method enables measurement of several scalar and residual dipolar couplings, which can potentially be used for structure determination of large proteins.
Original languageEnglish
Pages (from-to)127-133
Number of pages7
JournalJournal of Biomolecular NMR
Volume20
Issue number2
DOIs
Publication statusPublished - 2001
MoE publication typeA1 Journal article-refereed

Fingerprint

Spectrum Analysis
Spectroscopy
Proteins
Magnetic Fields
Magnetization
Carbon
Experiments
Nuclear magnetic resonance
Magnetic fields

Cite this

Permi, P. ; Annila, Arto. / A new approach for obtaining sequential assignment of large proteins. In: Journal of Biomolecular NMR. 2001 ; Vol. 20, No. 2. pp. 127-133.
@article{087f2ae08aaf416ab24c4255d19d705d,
title = "A new approach for obtaining sequential assignment of large proteins",
abstract = "A novel NMR experiment for obtaining sequential assignment of large proteins and protein complexes is described. The proposed method takes full advantage of transverse relaxation optimized spectroscopy (TROSY) and utilizes spin-state-selection to distinguish between intraresidual and sequential connectivities in the HNCA-TROSY-type correlation experiment. Thus, the intra- and interresidual cross peaks can be identified without relaying magnetization via carbonyl carbon, which relaxes very rapidly at the high magnetic fields where TROSY is most efficient. In addition, the presented method enables measurement of several scalar and residual dipolar couplings, which can potentially be used for structure determination of large proteins.",
author = "P. Permi and Arto Annila",
year = "2001",
doi = "10.1023/A:1011208803036",
language = "English",
volume = "20",
pages = "127--133",
journal = "Journal of Biomolecular NMR",
issn = "0925-2738",
publisher = "Springer",
number = "2",

}

A new approach for obtaining sequential assignment of large proteins. / Permi, P.; Annila, Arto.

In: Journal of Biomolecular NMR, Vol. 20, No. 2, 2001, p. 127-133.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - A new approach for obtaining sequential assignment of large proteins

AU - Permi, P.

AU - Annila, Arto

PY - 2001

Y1 - 2001

N2 - A novel NMR experiment for obtaining sequential assignment of large proteins and protein complexes is described. The proposed method takes full advantage of transverse relaxation optimized spectroscopy (TROSY) and utilizes spin-state-selection to distinguish between intraresidual and sequential connectivities in the HNCA-TROSY-type correlation experiment. Thus, the intra- and interresidual cross peaks can be identified without relaying magnetization via carbonyl carbon, which relaxes very rapidly at the high magnetic fields where TROSY is most efficient. In addition, the presented method enables measurement of several scalar and residual dipolar couplings, which can potentially be used for structure determination of large proteins.

AB - A novel NMR experiment for obtaining sequential assignment of large proteins and protein complexes is described. The proposed method takes full advantage of transverse relaxation optimized spectroscopy (TROSY) and utilizes spin-state-selection to distinguish between intraresidual and sequential connectivities in the HNCA-TROSY-type correlation experiment. Thus, the intra- and interresidual cross peaks can be identified without relaying magnetization via carbonyl carbon, which relaxes very rapidly at the high magnetic fields where TROSY is most efficient. In addition, the presented method enables measurement of several scalar and residual dipolar couplings, which can potentially be used for structure determination of large proteins.

U2 - 10.1023/A:1011208803036

DO - 10.1023/A:1011208803036

M3 - Article

VL - 20

SP - 127

EP - 133

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

SN - 0925-2738

IS - 2

ER -