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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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Publication details

The article was received on 11 Aug 2015, accepted on 14 Sep 2015 and first published on 21 Sep 2015


Article type: Communication
DOI: 10.1039/C5CP04765J
Citation: Phys. Chem. Chem. Phys., 2015,17, 27264-27269
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    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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