Northwestern Medicine scientists have developed a new experimental method to analyze conformational fluctuations in protein ...

Researchers have discovered how unstructured segments of surface proteins regulate the biological function of a cell. Their study, published in Nature Communications, sheds new light on the interplay ...

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 ...

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 ...

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 ...

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 ...

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 ...

A grayscale ribbon representation of a protein with space filling representations of a steroid (orange) and β-lactamase active site (green). One of the hormone-binding protein switches Credit: Kirill ...

A screen using in vitro-selected synthetic nanobodies identified inhibitors of SMC protein function in bacterial cells, revealing a coiled coil region as a vital component of the chromosome-folding ...