Every function in a cell is associated with a particular protein or group of proteins, typically in a well-defined three-dimensional structure. However, intrinsically disordered regions of proteins ...

Fusion oncoproteins arise when a gene fuses with another gene and acquires new abilities. Such abilities can include the formation of biomolecular condensates, "droplets" of concentrated proteins, DNA ...

Intrinsically disordered regions (IDRs) of proteins, when tethered to folded domains, function either as flexible tails or as linkers between domains. Most IDRs are composed of a mixture of oppositely ...

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” ...

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 ...

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, ...

Examining an intrinsically disordered protein: "Re" is the end-to-end distance or height, "Rg" is the radius of gyration or overall size. Proteins are essential for our human body functions. There are ...

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 ...

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 ...