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.

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 chemical characteristics. Many ...

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 ...

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 ...

A comprehensive analysis of over 500,000 human protein variants reveals that 60% of disease-causing missense mutations reduce protein stability In a recent study published in Nature, researchers used ...

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 ...

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 ...