English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Measurement and ab initio calculation of CSA/dipole- dipole cross-correlated relaxation provide insight into the mechanism of a H-2-forming dehydrogenase

MPS-Authors
/persons/resource/persons254122

Bartoschek,  S.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254182

Buurman,  G.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254314

Griesinger,  C.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Bartoschek, S., Buurman, G., Geierstanger, B. H., Lapham, J., & Griesinger, C. (2003). Measurement and ab initio calculation of CSA/dipole- dipole cross-correlated relaxation provide insight into the mechanism of a H-2-forming dehydrogenase. Journal of the American Chemical Society, 125(44), 13308-13309.


Cite as: http://hdl.handle.net/21.11116/0000-0007-C9AA-7
Abstract
There is no abstract available