Nasrollah Rezaei-Ghaleh, Frederik Klama, Francesca Munari, Markus Zweckstetter
Bioinformatics (Oxford, England) 2015 Apr 15A 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 HYdrodynamic CoUpling of Domains (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. The source code and documentation are available at www.mpibpc.mpg.de/106144/software. mzwecks@gwdg.de or nare@nmr.mpibpc.mpg.de Supplementary material is available at Bioinformatics online. © The Author 2014. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com.
Nasrollah Rezaei-Ghaleh, Frederik Klama, Francesca Munari, Markus Zweckstetter. HYCUD: a computational tool for prediction of effective rotational correlation time in flexible proteins. Bioinformatics (Oxford, England). 2015 Apr 15;31(8):1319-21
PMID: 25505088
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