High-Accuracy Residual 1HN-13C and 1HN-1HN Dipolar Couplings in Perdeuterated Proteins

Sebastian Meier, Daniel Haussinger, Pernille Rose Jensen, Marco Rogowski, Stephan Grzesiek

Research output: Contribution to journalJournal articleResearchpeer-review


Truncation by the presence of many short-range residual dipolar couplings (RDCs) hinders the observation of long-range RDCs in weakly aligned biomacromolecules. Perdeuteration of proteins followed by reprotonation of labile hydrogen positions greatly alleviates this problem. Here we show that for small perdeuterated proteins, a large number (up to 10 in protein G) of long-range RDCs to 13C and 1HN can be observed from individual amide protons. The 1HN ↔ 13C RDCs comprise correlations to 13Cα, 13Cβ, and 13C' nuclei of the same and the preceding amino acid, as well as 13C' nuclei of hydrogen-bonded amino acids. The accuracy of the coupling constants is very high and defines individual internuclear distances to within few picometers. Deviations between measured RDC values and values predicted from the 1.1 Å crystal structure of protein G are mainly found in two surface-exposed loop regions. The deviations show a strong correlation to the B-factor of the crystal structure. Copyright © 2003 American Chemical Society.
Original languageEnglish
JournalJournal of the American Chemical Society
Issue number1
Pages (from-to)44-45
Number of pages2
Publication statusPublished - 2003
Externally publishedYes


  • amino acid
  • carbon
  • hydrogen
  • protein
  • proton
  • article
  • calculation
  • chemical structure
  • crystal
  • crystal structure
  • dynamics
  • geometry
  • hydrogen bond
  • macromolecule
  • molecule
  • nuclear magnetic resonance
  • parameter
  • Amides
  • Carbon Isotopes
  • Deuterium
  • Nuclear Magnetic Resonance, Biomolecular
  • Proteins
  • 2D


Dive into the research topics of 'High-Accuracy Residual 1HN-13C and 1HN-1HN Dipolar Couplings in Perdeuterated Proteins'. Together they form a unique fingerprint.

Cite this