Magnetization Transfer via Residual Dipolar Couplings: Application to Proton-Proton Correlations in Partially Aligned Proteins

Maurizio Pellecchia; Craig W. Vander Kooi; Kai Keliikuli; Erik R.P. Zuiderweg

doi:10.1006/jmre.2000.2058

Magnetization Transfer via Residual Dipolar Couplings: Application to Proton-Proton Correlations in Partially Aligned Proteins

Maurizio Pellecchia, Craig W. Vander Kooi, Kai Keliikuli, Erik R.P. Zuiderweg

Research output: Contribution to journal › Editorial

9 Scopus citations

Abstract

A novel three-dimensional NMR experiment is reported that allows the observation of correlations between amide and other protons via residual dipolar couplings in partially oriented proteins. The experiment is designed to permit quantitative measurement of the magnitude of proton-proton residual dipolar couplings in larger molecules and at higher degree of alignments. The observed couplings contain data valuable for protein resonance assignment, local protein structure refinement, and determination of low-resolution protein folds.

Original language	English
Pages (from-to)	435-439
Number of pages	5
Journal	Journal of Magnetic Resonance
Volume	143
Issue number	2
DOIs	https://doi.org/10.1006/jmre.2000.2058
State	Published - Apr 2000

Bibliographical note

Funding Information:
The work was supported by NIH Grants GM52421 and GM52406. CWVK is the recipient of a University of Michigan Regents Fellowship. We thank Drs. C. Smith and M. A. Saper for preliminary coordinates of YopH. The W. M. Keck Foundation, NIH, NSF and Parke-Davis/Warner Lambert are gratefully acknowledged for financial support toward the 800 MHz NMR instrument.

Keywords

Homonuclear decoupling
Protein assignment
Protein structure
Residual dipolar coupling

ASJC Scopus subject areas

Biophysics
Biochemistry
Nuclear and High Energy Physics
Condensed Matter Physics

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10.1006/jmre.2000.2058

Cite this

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title = "Magnetization Transfer via Residual Dipolar Couplings: Application to Proton-Proton Correlations in Partially Aligned Proteins",

abstract = "A novel three-dimensional NMR experiment is reported that allows the observation of correlations between amide and other protons via residual dipolar couplings in partially oriented proteins. The experiment is designed to permit quantitative measurement of the magnitude of proton-proton residual dipolar couplings in larger molecules and at higher degree of alignments. The observed couplings contain data valuable for protein resonance assignment, local protein structure refinement, and determination of low-resolution protein folds.",

keywords = "Homonuclear decoupling, Protein assignment, Protein structure, Residual dipolar coupling",

author = "Maurizio Pellecchia and {Vander Kooi}, {Craig W.} and Kai Keliikuli and Zuiderweg, {Erik R.P.}",

note = "Funding Information: The work was supported by NIH Grants GM52421 and GM52406. CWVK is the recipient of a University of Michigan Regents Fellowship. We thank Drs. C. Smith and M. A. Saper for preliminary coordinates of YopH. The W. M. Keck Foundation, NIH, NSF and Parke-Davis/Warner Lambert are gratefully acknowledged for financial support toward the 800 MHz NMR instrument.",

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doi = "10.1006/jmre.2000.2058",

language = "English",

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T1 - Magnetization Transfer via Residual Dipolar Couplings

T2 - Application to Proton-Proton Correlations in Partially Aligned Proteins

AU - Pellecchia, Maurizio

AU - Vander Kooi, Craig W.

AU - Keliikuli, Kai

AU - Zuiderweg, Erik R.P.

N1 - Funding Information: The work was supported by NIH Grants GM52421 and GM52406. CWVK is the recipient of a University of Michigan Regents Fellowship. We thank Drs. C. Smith and M. A. Saper for preliminary coordinates of YopH. The W. M. Keck Foundation, NIH, NSF and Parke-Davis/Warner Lambert are gratefully acknowledged for financial support toward the 800 MHz NMR instrument.

PY - 2000/4

Y1 - 2000/4

N2 - A novel three-dimensional NMR experiment is reported that allows the observation of correlations between amide and other protons via residual dipolar couplings in partially oriented proteins. The experiment is designed to permit quantitative measurement of the magnitude of proton-proton residual dipolar couplings in larger molecules and at higher degree of alignments. The observed couplings contain data valuable for protein resonance assignment, local protein structure refinement, and determination of low-resolution protein folds.

AB - A novel three-dimensional NMR experiment is reported that allows the observation of correlations between amide and other protons via residual dipolar couplings in partially oriented proteins. The experiment is designed to permit quantitative measurement of the magnitude of proton-proton residual dipolar couplings in larger molecules and at higher degree of alignments. The observed couplings contain data valuable for protein resonance assignment, local protein structure refinement, and determination of low-resolution protein folds.

KW - Homonuclear decoupling

KW - Protein assignment

KW - Protein structure

KW - Residual dipolar coupling

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Magnetization Transfer via Residual Dipolar Couplings: Application to Proton-Proton Correlations in Partially Aligned Proteins

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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