RNA-binding proteins use a dual binding mechanism involving zinc finger (ZnF) domains and intrinsically disordered regions (IDR), reports a new study from Institute of Science Tokyo, Japan. Using ...

Scientists have discovered a new way to advance drug discovery and diagnostics by targeting a part of the proteome (the complete set of proteins in an organism) that was previously thought ...

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, scientists have relied on structure to understand protein function. Tools like AlphaFold have revolutionized how researchers predict and design folded proteins, allowing for new ...

In Greek mythology, Proteus, son of Poseidon and prophetic shepherd of sea-beasts, could foretell the future. The elusive sea god was difficult to capture as he assumed many forms—a lion, a serpent, ...

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 ...

Deep learning tools for protein design can also be used to create molecules that bind to them. Certain peptides, such as intrinsically disordered proteins (IDPs), are challenging to target due to ...

Intrinsically disordered proteins must compete for binding to common regulatory targets to carry out their biological functions. Previously, we showed that the activation domains of two disordered ...

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 ...