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Issue 41, 2015
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Energetic and topological determinants of a phosphorylation-induced disorder-to-order protein conformational switch

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Abstract

We show that the phosphorylation of 4E-BP2 acts as a triggering event to shape its folding-function landscape that is delicately balanced between conflicting favorable energetics and intrinsically unfavorable topological connectivity. We further provide first evidence that the fitness landscapes of proteins at the threshold of disorder can differ considerably from ordered domains.

Graphical abstract: Energetic and topological determinants of a phosphorylation-induced disorder-to-order protein conformational switch

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Article information


Submitted
11 Aug 2015
Accepted
14 Sep 2015
First published
21 Sep 2015

Phys. Chem. Chem. Phys., 2015,17, 27264-27269
Article type
Communication

Energetic and topological determinants of a phosphorylation-induced disorder-to-order protein conformational switch

S. Gopi, N. Rajasekaran, A. Singh, S. Ranu and A. N. Naganathan, Phys. Chem. Chem. Phys., 2015, 17, 27264
DOI: 10.1039/C5CP04765J

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