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Structural biases in disordered proteins are prevalent in the cell

Nat Struct Mol Biol. 2024-01; 
David Moses, Karina Guadalupe, Feng Yu, Eduardo Flores, Anthony R Perez, Ralph McAnelly, Nora M Shamoon, Gagandeep Kaur, Estefania Cuevas-Zepeda, Andrea D Merg, Erik W Martin, Alex S Holehouse, Shahar Sukenik
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Gene Synthesis … Genes encoding for IDP regions were obtained from GenScript and ligated between the two FPs using 5′ SacI and 3′ HindIII restriction sites. Cloned plasmids were amplified in XL1 … Get A Quote

摘要

Intrinsically disordered proteins and protein regions (IDPs) are prevalent in all proteomes and are essential to cellular function. Unlike folded proteins, IDPs exist in an ensemble of dissimilar conformations. Despite this structural plasticity, intramolecular interactions create sequence-specific structural biases that determine an IDP ensemble's three-dimensional shape. Such structural biases can be key to IDP function and are often measured in vitro, but whether those biases are preserved inside the cell is unclear. Here we show that structural biases in IDP ensembles found in vitro are recapitulated inside human-derived cells. We further reveal that structural biases can change in a sequence-dependent mann... More

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