Imagine trying to design a key for a lock that is constantly changing its shape. That is the exact challenge we face in ...

Molecular dynamics simulations yield thermodynamic and time-dependent behavior, elucidating the role of intrinsically disordered protein hydrophobicity and patterning in modulating biomolecular ...

Intrinsically disordered proteins (IDPs) can be challenging to identify and study due to their characteristic lack of structure. Bioinformatics techniques have been developed to predict whether a ...

Different DNA Structures Nucleate the Folding of Proteins to form specific complexes that modulate the readout of ...

For most proteins, structure is function. The complex three-dimensional shapes that proteins adopt create folds and pockets that can accomplish the remarkably improbable: driving chemical reactions ...

In synthetic and structural biology, advances in artificial intelligence have led to an explosion of designing new proteins with specific functions, from antibodies to blood clotting agents, by using ...

Intrinsically disordered proteins (IDPs) make up about 30 percent of our proteome. They are important to many fundamental aspects of biology and disrupted in disease. Since they lack a stable shape, ...

For decades, structural biologists shoved what looked like shoddy data in the back of their closets, embarrassed. While attempting to gather the structures of proteins, they would sometimes find that ...