![Figure 1 from Folding and Binding of an Intrinsically Disordered Protein: Fast, but Not 'Diffusion-Limited' | Semantic Scholar Figure 1 from Folding and Binding of an Intrinsically Disordered Protein: Fast, but Not 'Diffusion-Limited' | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/272a270594fb45860351c359d8a9fcd7725fbc54/2-Figure1-1.png)
Figure 1 from Folding and Binding of an Intrinsically Disordered Protein: Fast, but Not 'Diffusion-Limited' | Semantic Scholar
![PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis | Nature Chemical Biology PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis | Nature Chemical Biology](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fnchembio.1166/MediaObjects/41589_2013_Article_BFnchembio1166_Fig2_HTML.jpg)
PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis | Nature Chemical Biology
PUMA residual structure depends on its interaction with solution. (a)... | Download Scientific Diagram
![Coupled Folding and Binding of the Disordered Protein PUMA Does Not Require Particular Residual Structure – topic of research paper in Biological sciences. Download scholarly article PDF and read for free on Coupled Folding and Binding of the Disordered Protein PUMA Does Not Require Particular Residual Structure – topic of research paper in Biological sciences. Download scholarly article PDF and read for free on](https://cyberleninka.org/viewer_images/158553/f/1.png)
Coupled Folding and Binding of the Disordered Protein PUMA Does Not Require Particular Residual Structure – topic of research paper in Biological sciences. Download scholarly article PDF and read for free on
![Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein | PNAS Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein | PNAS](https://www.pnas.org/content/111/43/15420/F1.large.jpg)