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Plos Computational Biology : on the Importance of Polar Interactions for Complexes Containing Intrinsically Disordered Proteins, Volume 9

By Wong, Eric, T. C.

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Book Id: WPLBN0003952605
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos Computational Biology : on the Importance of Polar Interactions for Complexes Containing Intrinsically Disordered Proteins, Volume 9  
Author: Wong, Eric, T. C.
Volume: Volume 9
Language: English
Subject: Journals, Science, Computational Biology
Collections: Periodicals: Journal and Magazine Collection (Contemporary), PLoS Computational Biology
Historic
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Publisher: Plos

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C. Won, E. T. (n.d.). Plos Computational Biology : on the Importance of Polar Interactions for Complexes Containing Intrinsically Disordered Proteins, Volume 9. Retrieved from http://www.ebooklibrary.org/


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Description : There is a growing recognition for the importance of proteins with large intrinsically disordered (ID) segments in cell signaling and regulation. ID segments in these proteins often harbor regions that mediate molecular recognition. Coupled folding and binding of the recognition regions has been proposed to confer high specificity to interactions involving ID segments. However, researchers recently questioned the origin of the interaction specificity of ID proteins because of the overrepresentation of hydrophobic residues in their interaction interfaces. Here, we focused on the role of polar and charged residues in interactions mediated by ID segments. Making use of the extended nature of most ID segments when in complex with globular proteins, we first identified large numbers of complexes between globular proteins and ID segments by using radius-of-gyration-based selection criteria. Consistent with previous studies, we found the interfaces of these complexes to be enriched in hydrophobic residues, and that these residues contribute significantly to the stability of the interaction interface. However, our analyses also show that polar interactions play a larger role in these complexes than in structured protein complexes. Computational alanine scanning and salt-bridge analysis indicate that interfaces in ID complexes are highly complementary with respect to electrostatics, more so than interfaces of globular proteins. Follow-up calculations of the electrostatic contributions to the free energy of binding uncovered significantly stronger Coulombic interactions in complexes harbouring ID segments than in structured protein complexes. However, they are counter-balanced by even higher polardesolvation penalties. We propose that polar interactions are a key contributing factor to the observed high specificity of ID segment-mediated interactions.


 

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