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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-D98F-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-EE5B-8
Genre: Journal Article

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 Creators:
Salmon, L., Author
Bouvignies, G., Author
Marwick, P., Author
Lakomek, N. A.1, Author              
Showalter, S., Author
Li, D. W., Author
Walter, K.1, Author              
Griesinger, C.1, Author              
Brueschweiler, R., Author
Blackledge, M., Author
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: Gaussian axial fluctuation; molecular dynamics; NMR spectroscopy; protein dynamics; residual dipolar coupling
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Language(s): eng - English
 Dates: 2009
 Publication Status: Published in print
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Title: Angewandte Chemie International Edition
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 48 (23) Sequence Number: - Start / End Page: 4154 - 4157 Identifier: -