A protein engineered by University of Washington scientists wraps around its target. (Institute for Protein Design Image) The wiggly targets known to scientists as “intrinsically disordered proteins” ...

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, ...

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 ...

Textbooks often depict proteins in one conformation, but real life, as usual, is much messier. While some proteins have stable, unchanging structures, many others have intrinsically disordered regions ...

Imagine trying to design a key for a lock that is constantly changing its shape. That is the exact challenge we face in modern drug discovery when dealing with intrinsically disordered proteins. For ...

A new LMU study shows how proteins function reliably even without a stable 3D structure – and the crucial importance not only of short sequence motifs, but also of the chemical characteristics. Many ...

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 ...

The wiggly targets known to scientists as “intrinsically disordered proteins” have for decades eluded capture by custom-made drugs and antibodies. But they played such important biological roles — ...

Researchers at Harvard and Northwestern have developed a machine learning method that can design intrinsically disordered proteins with custom properties, addressing nearly 30% of all human proteins ...