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

MPG-Autoren
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Rezaei-Ghaleh,  N.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Munari,  F.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

Externe Ressourcen

http://bioinformatics.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=25505088
(Verlagsversion)

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2079532_Suppl.pdf
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Zitation

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.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-5CE3-4
Zusammenfassung
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.