On the performance of spin diffusion NMR techniques in oriented solids

Prospects for resonance assignments and distance measurements from separated local field experiments

Nathaniel Traaseth, T. Gopinath, Gianluigi Veglia

Research output: Contribution to journalArticle

Abstract

NMR spin diffusion experiments have the potential to provide both resonance assignment and internuclear distances for protein structure determination in oriented solid-state NMR. In this paper, we compared the efficiencies of three spin diffusion experiments: proton-driven spin diffusion (PDSD), cross-relaxation-driven spin diffusion (CRDSD), and proton-mediated proton transfer (PMPT). As model systems for oriented proteins, we used single crystals of N-acetyl-L-15N-leucine (NAL) and N-acetyl-L-15N-valyl- L-15N-leucine (NAVL) to probe long and short distances, respectively. We demonstrate that, for short 15N/15N distances such as those found in NAVL (3.3 Å), the PDSD mechanism gives the most intense cross-peaks, while, for longer distances (>6.5 Å), the CRDSD and PMPT experiments are more efficient. The PDSD was highly inefficient for transferring magnetization across distances greater than 6.5 Å (NAL crystal sample), due to small 15N/15N dipolar couplings (<4.5 Hz). Interestingly, the mismatched Hartmann-Hahn condition present in the PMPT experiment gave more intense cross-peaks for lower 1H and 15N RF spinlock amplitudes (32 and 17 kHz, respectively) rather than higher values (55 and 50 kHz), suggesting a more complex magnetization transfer mechanism. Numerical simulations are in good agreement with the experimental findings, suggesting a combined PMPT and CRDSD effect. We conclude that, in order to assign SLF spectra and measure shortand long-range distances, the combined use of homonuclear correlation spectra, such as the ones surveyed in this work, are necessary.

Original languageEnglish (US)
Pages (from-to)13872-13880
Number of pages9
JournalJournal of Physical Chemistry B
Volume114
Issue number43
DOIs
StatePublished - Nov 4 2010

Fingerprint

Distance measurement
Protons
Nuclear magnetic resonance
nuclear magnetic resonance
Proton transfer
protons
leucine
Experiments
Leucine
cross relaxation
Magnetization
Proteins
proteins
magnetization
Single crystals
Crystals
Computer simulation
solid state

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

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title = "On the performance of spin diffusion NMR techniques in oriented solids: Prospects for resonance assignments and distance measurements from separated local field experiments",
abstract = "NMR spin diffusion experiments have the potential to provide both resonance assignment and internuclear distances for protein structure determination in oriented solid-state NMR. In this paper, we compared the efficiencies of three spin diffusion experiments: proton-driven spin diffusion (PDSD), cross-relaxation-driven spin diffusion (CRDSD), and proton-mediated proton transfer (PMPT). As model systems for oriented proteins, we used single crystals of N-acetyl-L-15N-leucine (NAL) and N-acetyl-L-15N-valyl- L-15N-leucine (NAVL) to probe long and short distances, respectively. We demonstrate that, for short 15N/15N distances such as those found in NAVL (3.3 {\AA}), the PDSD mechanism gives the most intense cross-peaks, while, for longer distances (>6.5 {\AA}), the CRDSD and PMPT experiments are more efficient. The PDSD was highly inefficient for transferring magnetization across distances greater than 6.5 {\AA} (NAL crystal sample), due to small 15N/15N dipolar couplings (<4.5 Hz). Interestingly, the mismatched Hartmann-Hahn condition present in the PMPT experiment gave more intense cross-peaks for lower 1H and 15N RF spinlock amplitudes (32 and 17 kHz, respectively) rather than higher values (55 and 50 kHz), suggesting a more complex magnetization transfer mechanism. Numerical simulations are in good agreement with the experimental findings, suggesting a combined PMPT and CRDSD effect. We conclude that, in order to assign SLF spectra and measure shortand long-range distances, the combined use of homonuclear correlation spectra, such as the ones surveyed in this work, are necessary.",
author = "Nathaniel Traaseth and T. Gopinath and Gianluigi Veglia",
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T1 - On the performance of spin diffusion NMR techniques in oriented solids

T2 - Prospects for resonance assignments and distance measurements from separated local field experiments

AU - Traaseth, Nathaniel

AU - Gopinath, T.

AU - Veglia, Gianluigi

PY - 2010/11/4

Y1 - 2010/11/4

N2 - NMR spin diffusion experiments have the potential to provide both resonance assignment and internuclear distances for protein structure determination in oriented solid-state NMR. In this paper, we compared the efficiencies of three spin diffusion experiments: proton-driven spin diffusion (PDSD), cross-relaxation-driven spin diffusion (CRDSD), and proton-mediated proton transfer (PMPT). As model systems for oriented proteins, we used single crystals of N-acetyl-L-15N-leucine (NAL) and N-acetyl-L-15N-valyl- L-15N-leucine (NAVL) to probe long and short distances, respectively. We demonstrate that, for short 15N/15N distances such as those found in NAVL (3.3 Å), the PDSD mechanism gives the most intense cross-peaks, while, for longer distances (>6.5 Å), the CRDSD and PMPT experiments are more efficient. The PDSD was highly inefficient for transferring magnetization across distances greater than 6.5 Å (NAL crystal sample), due to small 15N/15N dipolar couplings (<4.5 Hz). Interestingly, the mismatched Hartmann-Hahn condition present in the PMPT experiment gave more intense cross-peaks for lower 1H and 15N RF spinlock amplitudes (32 and 17 kHz, respectively) rather than higher values (55 and 50 kHz), suggesting a more complex magnetization transfer mechanism. Numerical simulations are in good agreement with the experimental findings, suggesting a combined PMPT and CRDSD effect. We conclude that, in order to assign SLF spectra and measure shortand long-range distances, the combined use of homonuclear correlation spectra, such as the ones surveyed in this work, are necessary.

AB - NMR spin diffusion experiments have the potential to provide both resonance assignment and internuclear distances for protein structure determination in oriented solid-state NMR. In this paper, we compared the efficiencies of three spin diffusion experiments: proton-driven spin diffusion (PDSD), cross-relaxation-driven spin diffusion (CRDSD), and proton-mediated proton transfer (PMPT). As model systems for oriented proteins, we used single crystals of N-acetyl-L-15N-leucine (NAL) and N-acetyl-L-15N-valyl- L-15N-leucine (NAVL) to probe long and short distances, respectively. We demonstrate that, for short 15N/15N distances such as those found in NAVL (3.3 Å), the PDSD mechanism gives the most intense cross-peaks, while, for longer distances (>6.5 Å), the CRDSD and PMPT experiments are more efficient. The PDSD was highly inefficient for transferring magnetization across distances greater than 6.5 Å (NAL crystal sample), due to small 15N/15N dipolar couplings (<4.5 Hz). Interestingly, the mismatched Hartmann-Hahn condition present in the PMPT experiment gave more intense cross-peaks for lower 1H and 15N RF spinlock amplitudes (32 and 17 kHz, respectively) rather than higher values (55 and 50 kHz), suggesting a more complex magnetization transfer mechanism. Numerical simulations are in good agreement with the experimental findings, suggesting a combined PMPT and CRDSD effect. We conclude that, in order to assign SLF spectra and measure shortand long-range distances, the combined use of homonuclear correlation spectra, such as the ones surveyed in this work, are necessary.

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