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  Predicting the rotational tumbling of dynamic multidomain proteins and supramolecular complexes.

Rezaei-Ghaleh, N., Klama, F., Munari, F., & Zweckstetter, M. (2013). Predicting the rotational tumbling of dynamic multidomain proteins and supramolecular complexes. Angewandte Chemie International Edition, 52(43), 11410-11414. doi:10.1002/anie.201305094.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-87F4-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-D0C0-2
Genre: Journal Article

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1943473.pdf (Publisher version), 487KB
 
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 Creators:
Rezaei-Ghaleh, N.1, Author              
Klama, F., Author
Munari, F.1, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: hydrodynamic coupling; NMR spectroscopy; protein disorder; proteins; rotational diffusion
 Abstract: Time is of the essence: The rotational motion of biomolecules depends on intra- and intermolecular interactions and thus on distinct functional states. A new method, called HYCUD accurately predicts rotational correlation times in complex dynamic systems. It gives insights into the motional behavior of multidomain proteins in their free form and in supramolecular complexes.

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Language(s): eng - English
 Dates: 2013-09-022013-10-18
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201305094
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 52 (43) Sequence Number: - Start / End Page: 11410 - 11414 Identifier: -