AI Article Synopsis
- The phosphorylation of 4E-BP2 changes its structural and functional properties, impacting how it folds.
- This process reveals a balance between energy favorability and structural challenges.
- New evidence suggests that proteins near disorder have different "fitness landscapes" (how they function and maintain stability) compared to more organized proteins.
Article 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.
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| http://dx.doi.org/10.1039/c5cp04765j | DOI Listing |
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