In a paper published in Proceedings of the National Academy of Sciences, researchers from Technion and Tel Aviv University ...

Adhesion G protein-coupled receptors (GPCRs) are a group of cell-surface sensors associated with many body functions and diseases. However, they are not yet sufficiently understood to be exploited for ...

In a recent study published in the journal Nature Machine Intelligence, researchers developed "DeepGO-SE," a method to predict gene ontology (GO) functions from protein sequences using a large, ...

Northwestern Medicine scientists have developed a new experimental method to analyze conformational fluctuations in protein domains on a uniquely large scale, which may improve data-driven modeling, ...

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 ...

Low-complexity domains in proteins are composed of a small subset of the full complement of amino acids, and in these domains, the amino acid sequences are often repetitive. Their relevance to health ...

It has long been thought that protein function and stability are highly sensitive to changes in the composition of the internal structures, or protein cores. However, a large-scale experiment probing ...

Most mutations that cause disease by swapping one amino acid out for another do so by making the protein less stable, according to a major study of human protein variants that was published in Nature ...

Proteins are most well-known for their intricate structures. The α-helices and β-sheets that form from interactions between sidechains create distinct shapes that, along with the specific amino acid ...

The Human Domainome 1—the largest library of human protein variants—reveals the cause of certain genetic disorders, paving the way for personalized medicines. “We measured every possible mutation in ...