NMR h3JNC' couplings provide comprehensive geometrical constraints for protein H-bonds in solution

Nenad Juranić, Martin C. Moncrieffe, Elena Atanasova, Slobodan I Macura, Franklyn G. Prendergast

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Protein backbone H-bonds (>N-H⋯O-C<) show relationships between NMR h3JNC' couplings measured in solution and H-bond geometry parameters seen in X-ray crystal structures. Assuming that the solution and crystal structure of protein backbone is the same, the h3JNC' couplings can be calibrated to provide good estimates of both angular and radial H-bond parameters in a solution. The crucial premise of equality between the solution and the crystal structure of protein backbone we validated on the level of the NH-bonds orientation, by comparing the orientations inferred from X-ray crystal structures with the solution ones determined from NMR residual dipolar couplings.

Original languageEnglish (US)
Pages (from-to)503-507
Number of pages5
JournalCroatica Chemica Acta
Volume79
Issue number3
StatePublished - 2006

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Nuclear magnetic resonance
Crystal structure
Proteins
X rays
Crystal orientation
Geometry

Keywords

  • H-bond geometry
  • Hydrogen bonding
  • NMR
  • Proteins
  • Spin-spin couplings

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Juranić, N., Moncrieffe, M. C., Atanasova, E., Macura, S. I., & Prendergast, F. G. (2006). NMR h3JNC' couplings provide comprehensive geometrical constraints for protein H-bonds in solution. Croatica Chemica Acta, 79(3), 503-507.

NMR h3JNC' couplings provide comprehensive geometrical constraints for protein H-bonds in solution. / Juranić, Nenad; Moncrieffe, Martin C.; Atanasova, Elena; Macura, Slobodan I; Prendergast, Franklyn G.

In: Croatica Chemica Acta, Vol. 79, No. 3, 2006, p. 503-507.

Research output: Contribution to journalArticle

Juranić, N, Moncrieffe, MC, Atanasova, E, Macura, SI & Prendergast, FG 2006, 'NMR h3JNC' couplings provide comprehensive geometrical constraints for protein H-bonds in solution', Croatica Chemica Acta, vol. 79, no. 3, pp. 503-507.
Juranić, Nenad ; Moncrieffe, Martin C. ; Atanasova, Elena ; Macura, Slobodan I ; Prendergast, Franklyn G. / NMR h3JNC' couplings provide comprehensive geometrical constraints for protein H-bonds in solution. In: Croatica Chemica Acta. 2006 ; Vol. 79, No. 3. pp. 503-507.
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AU - Prendergast, Franklyn G.

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AB - Protein backbone H-bonds (>N-H⋯O-C<) show relationships between NMR h3JNC' couplings measured in solution and H-bond geometry parameters seen in X-ray crystal structures. Assuming that the solution and crystal structure of protein backbone is the same, the h3JNC' couplings can be calibrated to provide good estimates of both angular and radial H-bond parameters in a solution. The crucial premise of equality between the solution and the crystal structure of protein backbone we validated on the level of the NH-bonds orientation, by comparing the orientations inferred from X-ray crystal structures with the solution ones determined from NMR residual dipolar couplings.

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