Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.

@article{Amo2010QuantificationOP,
  title={Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.},
  author={Juan-Miguel Lopez del Amo and Uwe Fink and Bernd Reif},
  journal={Journal of biomolecular NMR},
  year={2010},
  volume={48 4},
  pages={203-12}
}
We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that backbone amides in the microcrystalline α-spectrin SH3 domain exchange rather slowly with the solvent (with exchange rates negligible within the individual (15)N-T (1) timescales). We observed chemical exchange for 6 residues with… CONTINUE READING
2 Citations
57 References
Similar Papers

References

Publications referenced by this paper.
Showing 1-10 of 57 references

Hydrogen exchange in peptides and proteins using NMR-spectroscopy

  • CE Dempsey
  • Prog Nucl Magn Reson Spectrosc
  • 2001
Highly Influential
6 Excerpts

Exchange rates by nuclear magnetic multiple resonance. 3. Exchange reactions in systems with several nonequivalent sites

  • S Forsen, RA Hoffman
  • J Chem Phys 40:1189–1190
  • 1964
Highly Influential
3 Excerpts

Hydrogen/deuterium isotope effects on the N-15 NMR chemical shifts and geometries of low-barrier hydrogen bonds in the solid state

  • H Benedict, C Hoelger, +4 authors HH Limbach
  • J Molec Struct
  • 1996
Highly Influential
4 Excerpts

Measurement of fast proton-exchange rates in isotopically labeled compounds

  • G Gemmecker, W Jahnke, H Kessler
  • J Am Chem
  • 1993
Highly Influential
4 Excerpts

Similar Papers

Loading similar papers…