Most proteins have no trouble folding quickly and efficiently to their native state.
However, an increasing number of diseases such as emphysema, Alzheimer s and Huntington s disease are associated with the failure of proteins to fold correctly. Variants of the serpin, antitrypsin, misfold and accumulate in the endoplasmic reticulum of hepatocyte cells, leading to a plasma deficiency and hepatocyte damage due to the accumulation of aggregated protein, leading to cirrhosis and emphysema. At least eight neurodegenerative disorders are caused by an expanded polyglutamine tract in the various disease proteins, including Huntington s disease and spinocerebellar ataxia type 3. Polyglutamine expansion causes the disease protein to misfold and aggregate, ultimately leading to neuronal death. All of our projects benefit greatly from their collaborative nature with other research groups within Monash and elsewhere.