All proteins must fold to their correct three-dimensional shape to function. However, changes in the sequence of the protein can disrupt this process, leading to self-association of the protein and disease. The polyglutamine repeat family of proteins are involved in a range of neurodegenerative disorders, the most common being Huntington s disease. In healthy individuals up to 40 glutamine repeats can be tolerated in many of these proteins, however, in diseased individuals glutamine repeats in excess of 45 are always observed. In this project we will determine the molecular mechanisms by which polyglutamine tract expansion causes the protein to aggregate and cause disease.
|Effective start/end date||2/01/07 → 31/12/09|
- Australian Research Council (ARC): AUD300,000.00