The Influence of a Scalar-Coupled Deuterium upon the Relaxation of a 15N Nucleus and Its Possible Exploitation as a Probe for Side-Chain Interactions in Proteins

Jonathan Boyd, Tapas K. Mal, Nick Soffe, Iain D. Campbell

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The magnitude of the quadrupole coupling constant (e2Qq1ℏ) of a deuteron is a good probe for hydrogen bonding. In protein structures, hydrogen-bonding interactions between side chains, between side chains and ligands, and between side chains and solvent are frequently found. An experiment that detects, via scalar coupling, the influence of a deuteron on the 15N nucleus of asparagine or glutamine side chains is presented. The experiment depends upon the resolution of the 1Δ15N (D) isotope shifts that allow the various isotopomers and isotopologues to be distinguished when 15N-labeled samples are dissolved in solvent mixtures of H2O/D2O. 15N lineshapes with theoretical simulations that provide estimates for the 2H quadrupole coupling constants are presented. The influence of 15N-2H dipolar-quadrupole cross correlation and the resulting small frequency shifts in the 15N multiplet are resolved in some of the spectra. The experimental data are provided using the free amino acids asparagine and glutamine for which the side chains were isotopicafly enriched in 15N and the recombinant pair of modules, flbronectin type 1 and epidermal growth factor, (F1-G) of tissue plasminogen activator, which were uniformly isotopically enriched in 15N.

Original languageEnglish (US)
Pages (from-to)61-71
Number of pages11
JournalJournal of Magnetic Resonance
Volume124
Issue number1
DOIs
StatePublished - Jan 1997

Fingerprint

Deuterium
Asparagine
Hydrogen Bonding
exploitation
Glutamine
deuterium
Hydrogen bonds
scalars
proteins
nuclei
probes
glutamine
Tissue Plasminogen Activator
Epidermal Growth Factor
Isotopes
quadrupoles
Proteins
Experiments
interactions
deuterons

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics

Cite this

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title = "The Influence of a Scalar-Coupled Deuterium upon the Relaxation of a 15N Nucleus and Its Possible Exploitation as a Probe for Side-Chain Interactions in Proteins",
abstract = "The magnitude of the quadrupole coupling constant (e2Qq1ℏ) of a deuteron is a good probe for hydrogen bonding. In protein structures, hydrogen-bonding interactions between side chains, between side chains and ligands, and between side chains and solvent are frequently found. An experiment that detects, via scalar coupling, the influence of a deuteron on the 15N nucleus of asparagine or glutamine side chains is presented. The experiment depends upon the resolution of the 1Δ15N (D) isotope shifts that allow the various isotopomers and isotopologues to be distinguished when 15N-labeled samples are dissolved in solvent mixtures of H2O/D2O. 15N lineshapes with theoretical simulations that provide estimates for the 2H quadrupole coupling constants are presented. The influence of 15N-2H dipolar-quadrupole cross correlation and the resulting small frequency shifts in the 15N multiplet are resolved in some of the spectra. The experimental data are provided using the free amino acids asparagine and glutamine for which the side chains were isotopicafly enriched in 15N and the recombinant pair of modules, flbronectin type 1 and epidermal growth factor, (F1-G) of tissue plasminogen activator, which were uniformly isotopically enriched in 15N.",
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The Influence of a Scalar-Coupled Deuterium upon the Relaxation of a 15N Nucleus and Its Possible Exploitation as a Probe for Side-Chain Interactions in Proteins. / Boyd, Jonathan; Mal, Tapas K.; Soffe, Nick; Campbell, Iain D.

In: Journal of Magnetic Resonance, Vol. 124, No. 1, 01.1997, p. 61-71.

Research output: Contribution to journalArticle

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AB - The magnitude of the quadrupole coupling constant (e2Qq1ℏ) of a deuteron is a good probe for hydrogen bonding. In protein structures, hydrogen-bonding interactions between side chains, between side chains and ligands, and between side chains and solvent are frequently found. An experiment that detects, via scalar coupling, the influence of a deuteron on the 15N nucleus of asparagine or glutamine side chains is presented. The experiment depends upon the resolution of the 1Δ15N (D) isotope shifts that allow the various isotopomers and isotopologues to be distinguished when 15N-labeled samples are dissolved in solvent mixtures of H2O/D2O. 15N lineshapes with theoretical simulations that provide estimates for the 2H quadrupole coupling constants are presented. The influence of 15N-2H dipolar-quadrupole cross correlation and the resulting small frequency shifts in the 15N multiplet are resolved in some of the spectra. The experimental data are provided using the free amino acids asparagine and glutamine for which the side chains were isotopicafly enriched in 15N and the recombinant pair of modules, flbronectin type 1 and epidermal growth factor, (F1-G) of tissue plasminogen activator, which were uniformly isotopically enriched in 15N.

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