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Single-molecule optical tweezers reveals folding steps of the domain swapping mechanism of a protein

Biophys J. 2021-09; 
Andres Bustamante, Rodrigo Rivera, Martin Floor, Jorge Babul, Mauricio Baez
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Mutant Libraries … Genes encoding monomeric FoxP1 E45C/R126C and FoxP1-L-FoxP1 E45C/K217C (Supporting materials and methods) mutants were synthesized and purchased from GenScript (Piscataway, NJ). For both monomeric and fusion proteins, A39P mutants were generated using … Get A Quote

摘要

Domain swapping is a mechanism of protein oligomerization by which two or more subunits exchange structural elements to generate an intertwined complex. Numerous studies support a diversity of swapping mechanisms in which structural elements can be exchanged at different stages of the folding pathway of a subunit. Here, we used single-molecule optical tweezers technique to analyze the swapping mechanism of the forkhead DNA-binding domain of human transcription factor FoxP1. FoxP1 populates folded monomers in equilibrium with a swapped dimer. We generated a fusion protein linking two FoxP1 domains in tandem to obtain repetitive mechanical folding and unfolding trajectories. Thus, by stretching the same molecule ... More

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