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 ...

Protein activity can be precisely regulated via subtle changes in temperature using heat-sensitive switches. Underlying this ...

Many proteins have a complex architecture that enables biological functions. Molecules can bind to specific sites on a protein and alter its function. A team at HZB has now investigated the Nsp1 ...

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 ...

Unstable proteins are the main drivers of many different heritable diseases, according to a new study, including genetic disorders responsible for the formation of cataracts, and different types of ...

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 which cause disease by swapping one amino acid out for another do so by making the protein less stable, according to a massive study of human protein variants published today in the ...

When a protein folds, its string of amino acids wiggles and jiggles through countless conformations before it forms a fully folded, functional protein. This rapid and complex process is hard to ...

Many proteins have a complex architecture that enables biological functions. Molecules can bind to specific sites on a ...