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 ...
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 ...
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 ...
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 ...
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 ...
Protein dynamics and intrinsic disorder represent a paradigm shift in our understanding of protein structure and function. Rather than depending solely on a single stable three‐dimensional structure, ...
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 ...
Around 80 percent of proteins involved in diseases like cancer and neurodegenerative illnesses do not have a stable structure. These proteins, known as intrinsically disordered proteins (IDPs) can ...
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 ...
Researchers of Mainz University and EMBL Hamburg present a new approach to determine the form of disordered proteins by using two different methods simultaneously in a single sample. Proteins are ...
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