Examining the pH switch of copper-zinc superoxide dismutase mutant A4V

Amyotrophic lateral sclerosis(ALS) is a neurodegenerative disease that causes progressive loss to motor neurons. Buildup of superoxide anions (O2-) and aggregation of superoxide dismutase (SOD) is thought to be probable causes of damage to the neurons. This damage results in the progressive loss of function in the neurons resulting in flaccid paralysis. Superoxide anions were originally thought to cause irreparable damage to the motor neurons; however, recent studies have shown that the aggregation of SOD causes damage to the cell. Furthermore, the ability for the SOD1 to get metalated to dissuade aggregation has become an important topic of study in ALS research. In this study, human SOD1 A4V mutant was successfully expressed and purified and set for crystallization at various pH to understand the effect of minor pH changes on the stability of the protein structure. Future X-ray crystallography analysis could result in further understanding of how SOD1 aggregates which might help produce viable treatments for the familial form of ALS

Examining the pH switch of copper-zinc superoxide dismutase mutant A4V

Amyotrophic lateral sclerosis(ALS) is a neurodegenerative disease that causes progressive loss to motor neurons. Buildup of superoxide anions (O2-) and aggregation of superoxide dismutase (SOD) is thought to be probable causes of damage to the neurons. This damage results in the progressive loss of function in the neurons resulting in flaccid paralysis. Superoxide anions were originally thought to cause irreparable damage to the motor neurons; however, recent studies have shown that the aggregation of SOD causes damage to the cell. Furthermore, the ability for the SOD1 to get metalated to dissuade aggregation has become an important topic of study in ALS research. In this study, human SOD1 A4V mutant was successfully expressed and purified and set for crystallization at various pH to understand the effect of minor pH changes on the stability of the protein structure. Future X-ray crystallography analysis could result in further understanding of how SOD1 aggregates which might help produce viable treatments for the familial form of ALS