期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 17, 期 41, 页码 27264-27269出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5cp04765j
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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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