Calcium-binding proteins afford calibration of dihedral-angle dependence of 3JNCγ coupling constant in aspartate and asparagine residues

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

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Calibration of the 3JNCγ couplings across the N-Cα- Cβ-Cγ fragment of aspartate and asparagine residues is afforded by two interactions that produce fixed conformations of the side chains in solution. One is the binding of these side chains to calcium ions; the other is the H-bond interaction of these side chains with a backbone amide.

Original languageEnglish (US)
Pages (from-to)222-225
Number of pages4
JournalJournal of Magnetic Resonance
Volume175
Issue number2
DOIs
StatePublished - Aug 1 2005

Keywords

  • Asparagine
  • Aspartate
  • Calmodulin
  • Conformation
  • Metal binding
  • Nitrogen-carbon
  • Side chain
  • Spin-spin couplings
  • Vicinal couplings

ASJC Scopus subject areas

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

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