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

Salmon, L.; Bouvignies, G.; Marwick, P.; Lakomek, N. A.; Showalter, S.; Li, D. W.; Walter, K.; Griesinger, C.; Brueschweiler, R.; Blackledge, M.

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

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.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-D98F-D Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-EE5B-8

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Urheber:
Salmon, L., Autor
Bouvignies, G., Autor
Marwick, P., Autor
Lakomek, N. A.¹, Autor
Showalter, S., Autor
Li, D. W., Autor
Walter, K.¹, Autor
Griesinger, C.¹, Autor
Brueschweiler, R., Autor
Blackledge, M., Autor

Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567