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  HYCUD: A computational tool for prediction of effective rotational correlation time in flexible proteins.

Rezaei-Ghaleh, N., Klama, F., Munari, F., & Zweckstetter, M. (2015). HYCUD: A computational tool for prediction of effective rotational correlation time in flexible proteins. Bioinformatics, 31(8), 1319-1321. doi:10.1093/bioinformatics/btu824.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-5CE3-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-27BE-C
Genre: Journal Article

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2079532.pdf (Publisher version), 183KB
 
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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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 Abstract: MOTIVATION: A large fraction of eukaryotic proteins contain unstructured tails or linkers. The presence of flexible regions allows these systems to experience a high level of mobility facilitating their biological function. The complex nature of protein rotation in such flexible modular systems precludes a straightforward application of hydrodynamic methods to calculate their rotational motional properties. We describe the workflow of HYCUD, a program for prediction of effective rotational correlation times in multidomain proteins. The usage of HYCUD is demonstrated by its application to the ribosomal protein L7/L12. Rotational correlation times predicted by HYCUD might be used to detect molecular switch events mediated by disorder-order transitions in interdomain linkers. Availability: The source code and documentation are available at www.mpibpc.mpg.de/106144/software.

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Language(s): eng - English
 Dates: 2014-12-122015-04-15
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1093/bioinformatics/btu824
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Title: Bioinformatics
Source Genre: Journal
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Pages: - Volume / Issue: 31 (8) Sequence Number: - Start / End Page: 1319 - 1321 Identifier: -