English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.

MPS-Authors
/persons/resource/persons15147

Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

1478478.pdf
(Publisher version), 3MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Jensen, M. R., Markwick, P. R., Meier, S., Griesinger, C., Zweckstetter, M., Grzesiek, S., et al. (2009). Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. Structure, 17(9), 1169-1185. doi:10.1016/j.str.2009.08.001.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-9EA6-1
Abstract
There is no abstract available