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

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.

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1478478.pdf (Publisher version), 3MB
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Jensen, M. R., Author
Markwick, P. R., Author
Meier, S., Author
Griesinger, C.1, Author                 
Zweckstetter, M.2, Author           
Grzesiek, S., Author
Bernado, P., Author
Blackledge, M., Author
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Language(s): eng - English
 Dates: 2009-09-09
 Publication Status: Published online
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.str.2009.08.001
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Title: Structure
Source Genre: Journal
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Pages: - Volume / Issue: 17 (9) Sequence Number: - Start / End Page: 1169 - 1185 Identifier: -