NH-NH Vector Correlation in Peptides by Solid-State NMR

B. Reif; M. Hohwy; C. P. Jaroniec; C. M. Rienstra; R. G. Griffin

doi:10.1006/jmre.2000.2067

NH-NH Vector Correlation in Peptides by Solid-State NMR

B. Reif, M. Hohwy, C. P. Jaroniec, C. M. Rienstra, R. G. Griffin

Associate Professorship of Solid-State NMR spectroscopy

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

73 Scopus citations

Abstract

We present a novel solid-state magic angle-spinning NMR method for measuring the NH_i-NH_i+1 projection angle θ_i,i+1 in peptides. The experiment is applicable to uniformly ¹⁵N-labeled peptides and is demonstrated on the chemotactic tripeptide ^N-formyl-L-Met-L-Leu-L-Phe. The projection angle θ_i,i+1 is directly related to the peptide backbone torsion angles φ_i and ψ_i. The method utilizes the T-MREV recoupling scheme to restore ¹⁵N-¹H interactions, and proton-mediated spin diffusion to establish ¹⁵N-¹⁵N correlations. T-MREV has recently been shown to increase the dynamic range of the ¹⁵N-¹H recoupling by γ-encoding, and permits an accurate determination of the recoupled NH dipolar interaction. The results are interpreted in a quasi-analytical fashion that permits efficient extraction of the structural parameters.

Original language	English
Pages (from-to)	132-141
Number of pages	10
Journal	Journal of Magnetic Resonance
Volume	145
Issue number	1
DOIs	https://doi.org/10.1006/jmre.2000.2067
State	Published - Jul 2000

Keywords

Magic angle spinning (MAS) solid-state NMR; di
Polar vector correlation
Structure determination in peptides
T-MREV
γ-encoded heteronuclear recoupling and homonuclear decoupling

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title = "NH-NH Vector Correlation in Peptides by Solid-State NMR",

abstract = "We present a novel solid-state magic angle-spinning NMR method for measuring the NHi-NHi+1 projection angle θi,i+1 in peptides. The experiment is applicable to uniformly 15N-labeled peptides and is demonstrated on the chemotactic tripeptide N-formyl-L-Met-L-Leu-L-Phe. The projection angle θi,i+1 is directly related to the peptide backbone torsion angles φi and ψi. The method utilizes the T-MREV recoupling scheme to restore 15N-1H interactions, and proton-mediated spin diffusion to establish 15N-15N correlations. T-MREV has recently been shown to increase the dynamic range of the 15N-1H recoupling by γ-encoding, and permits an accurate determination of the recoupled NH dipolar interaction. The results are interpreted in a quasi-analytical fashion that permits efficient extraction of the structural parameters.",

keywords = "Magic angle spinning (MAS) solid-state NMR; di, Polar vector correlation, Structure determination in peptides, T-MREV, γ-encoded heteronuclear recoupling and homonuclear decoupling",

author = "B. Reif and M. Hohwy and Jaroniec, {C. P.} and Rienstra, {C. M.} and Griffin, {R. G.}",

note = "Funding Information: This research was supported by the NIH under Grants GM-23403 and RR-00995. B.R. acknowledges support from the Deutsche Forschungsgemein-schaft (Grant Re 1435/1-1). C.P.J. is a recipient of a NSF Predoctoral Fellowship. C.M.R. was a Howard Hughes Medical Institute Predoctoral Fellow.",

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T1 - NH-NH Vector Correlation in Peptides by Solid-State NMR

AU - Reif, B.

AU - Hohwy, M.

AU - Jaroniec, C. P.

AU - Rienstra, C. M.

AU - Griffin, R. G.

N1 - Funding Information: This research was supported by the NIH under Grants GM-23403 and RR-00995. B.R. acknowledges support from the Deutsche Forschungsgemein-schaft (Grant Re 1435/1-1). C.P.J. is a recipient of a NSF Predoctoral Fellowship. C.M.R. was a Howard Hughes Medical Institute Predoctoral Fellow.

PY - 2000/7

Y1 - 2000/7

N2 - We present a novel solid-state magic angle-spinning NMR method for measuring the NHi-NHi+1 projection angle θi,i+1 in peptides. The experiment is applicable to uniformly 15N-labeled peptides and is demonstrated on the chemotactic tripeptide N-formyl-L-Met-L-Leu-L-Phe. The projection angle θi,i+1 is directly related to the peptide backbone torsion angles φi and ψi. The method utilizes the T-MREV recoupling scheme to restore 15N-1H interactions, and proton-mediated spin diffusion to establish 15N-15N correlations. T-MREV has recently been shown to increase the dynamic range of the 15N-1H recoupling by γ-encoding, and permits an accurate determination of the recoupled NH dipolar interaction. The results are interpreted in a quasi-analytical fashion that permits efficient extraction of the structural parameters.

AB - We present a novel solid-state magic angle-spinning NMR method for measuring the NHi-NHi+1 projection angle θi,i+1 in peptides. The experiment is applicable to uniformly 15N-labeled peptides and is demonstrated on the chemotactic tripeptide N-formyl-L-Met-L-Leu-L-Phe. The projection angle θi,i+1 is directly related to the peptide backbone torsion angles φi and ψi. The method utilizes the T-MREV recoupling scheme to restore 15N-1H interactions, and proton-mediated spin diffusion to establish 15N-15N correlations. T-MREV has recently been shown to increase the dynamic range of the 15N-1H recoupling by γ-encoding, and permits an accurate determination of the recoupled NH dipolar interaction. The results are interpreted in a quasi-analytical fashion that permits efficient extraction of the structural parameters.

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KW - Structure determination in peptides

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NH-NH Vector Correlation in Peptides by Solid-State NMR

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