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  High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment.

Rumpel, S., Becker, S., & Zweckstetter, M. (2008). High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment. Journal of Biomolecular NMR, 40(1), 1-13. Retrieved from http://springerlink.metapress.com/content/15r81702p04t73p2/fulltext.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-DD4F-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-DD1D-E
Genre: Journal Article

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 Creators:
Rumpel, S.1, Author              
Becker, S.2, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: NMR solution structure; homodimer CylR2; paramagnetic relaxation enhancement; PALES; residual dipolar couplings; rigid-body docking
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Language(s): eng - English
 Dates: 2008-01
 Publication Status: Published in print
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 40 (1) Sequence Number: - Start / End Page: 1 - 13 Identifier: -