Genetic variations resulting in a change of amino acid sequence can have a dramatic effect
on stability, hydrogen bond network, conformational dynamics, activity and many other …

The native state of serpins represents a long-lived intermediate or metastable structure on
the serpin folding pathway. Upon interaction with a protease, the serpin trap is sprung and …

Expansion of “low complex” repeats of amino acids such as glutamine (Poly-Q) is associated
with protein misfolding and the development of degenerative diseases such as Huntington's …

The aggregation of ataxin-3 is associated with spinocerebellar ataxia type 3, which is
characterized by the formation of intraneuronal aggregates. However, the mechanism of …

Gram-negative pathogens commonly use the chaperone-usher pathway to assemble
adhesive multisubunit fibers on their surface. In the periplasm, subunits are stabilized by a …

Growing evidence suggests that aggregation-prone proteins are both harmful and functional
for a cell. How do cellular systems balance the detrimental and beneficial effect of protein …

Polyglutamine proteins that cause neurodegenerative disease are known to form
proteinaceous aggregates, such as nuclear inclusions, in the neurons of affected patients …

Ataxin-3 belongs to the family of polyglutamine proteins, which are associated with nine
different neurodegenerative disorders. Relatively little is known about the structural and …

The mechanisms by which a promiscuous protein can strongly interact with several different
proteins using the same binding interface are not completely understood. An example is …

α1-Antitrypsin is the prototypical member of the serine proteinase inhibitor or serpin
superfamily of proteins. The family includes α1-antichymotrypsin, C1 inhibitor, antithrombin …