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Journal Article

Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin.

MPS-Authors
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Lakomek,  N. A.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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

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

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Salmon, L., Bouvignies, G., Marwick, P., Lakomek, N. A., Showalter, S., Li, D. W., et al. (2009). Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin. Angewandte Chemie International Edition, 48(23), 4154-4157. Retrieved from http://www3.interscience.wiley.com/cgi-bin/fulltext/122372839/PDFSTART.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-D98F-D
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