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Human FoxP proteins share a highly conserved DNA‐binding domain that dimerizes via three‐dimensional domain swapping, although showing varying oligomerization propensities among its members. Here, we present an experimental and computational characterization of all human FoxP proteins to unravel how their amino acid substitutions impact their folding and dimerization mechanism. We solved the crystal...
Cold shock proteins (Csp) constitute a family of ubiquitous small proteins that act as RNA‐chaperones to avoid cold‐induced termination of translation. All members contain two subdomains composed of 2 and 3 β‐strands, respectively, which are connected by a hinge loop and fold into a β‐barrel. Bacillus caldolyticus Csp (BcCsp) is one of the most studied members of the family in terms of its folding,...
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