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 ...

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 ...

Ixr1 is a yeast transcriptional regulator previously identified as a player in the response to stress conditions, such as oxidative stress, hypoxia, iron limitation or DNA damage. Little is known ...

The alternative text for this image may have been generated using AI. Fig. 2: The cyclin D1 E-rich region is necessary for the recognition of H2B S14P in Microscale Thermophoresis (MST) analysis. The ...

Intrinsically disordered proteins (IDPs) are widely found in the proteomes of eukaryotes and play key roles in life processes such as transcription of genetic information and signaling. Apart from ...

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, ...

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 ...

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 ...

Shapeshifting proteins challenge a long-standing maxim in biology. A series of rodent experiments showed that even with abundant food and water, personal space is essential to prevent societal ...

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 ...