Event Title

Comparing the Sequence and Protein Structure Characteristics of Wild Type Copper-Zinc Superoxide Dismutase and Several Mutant Genotypes Commonly Associated with ALS

Session Number

Q17

Advisor(s)

Sarah Oleary, Illinois Mathematics and Science Academy

Location

B-116

Start Date

28-4-2016 12:45 PM

End Date

28-4-2016 1:10 PM

Disciplines

Neuroscience and Neurobiology

Abstract

The underlying cause of amyotrophic lateral sclerosis (ALS), a progressive neurodegenerative disease characterized by the selective death of motor neurons in the brain and spinal cord, is unclear. Scientists believe that approximately 20% of familial ALS is affected by the mutated copper-zinc superoxide dismutase (SOD1); however, how SOD1 causes ALS remains unknown. To gain a better understanding of the enzyme, we looked at multiple mutant structures and compared their protein characteristics to determine how certain mutations affect normal SOD1. We were able to find the secondary and tertiary structure of five mutant structures using the Molecular Modelling Database and Cn3D, an interactive examination of the sequence structure relationship using the National Center for Biotechnology Information database. We found that the original variants of SOD1 had specific point mutations associated with them along with specific differences in their secondary and tertiary structures. These changes included differences in the number of sulfate, copper, and zinc ions and the number of chains and interactions that formed the structure. The structural changes of SOD1 may cause it to gain a toxic property resulting in ALS. A further, more detailed analysis of the misfolded proteins may help answer how SOD1 could cause ALS.


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Apr 28th, 12:45 PM Apr 28th, 1:10 PM

Comparing the Sequence and Protein Structure Characteristics of Wild Type Copper-Zinc Superoxide Dismutase and Several Mutant Genotypes Commonly Associated with ALS

B-116

The underlying cause of amyotrophic lateral sclerosis (ALS), a progressive neurodegenerative disease characterized by the selective death of motor neurons in the brain and spinal cord, is unclear. Scientists believe that approximately 20% of familial ALS is affected by the mutated copper-zinc superoxide dismutase (SOD1); however, how SOD1 causes ALS remains unknown. To gain a better understanding of the enzyme, we looked at multiple mutant structures and compared their protein characteristics to determine how certain mutations affect normal SOD1. We were able to find the secondary and tertiary structure of five mutant structures using the Molecular Modelling Database and Cn3D, an interactive examination of the sequence structure relationship using the National Center for Biotechnology Information database. We found that the original variants of SOD1 had specific point mutations associated with them along with specific differences in their secondary and tertiary structures. These changes included differences in the number of sulfate, copper, and zinc ions and the number of chains and interactions that formed the structure. The structural changes of SOD1 may cause it to gain a toxic property resulting in ALS. A further, more detailed analysis of the misfolded proteins may help answer how SOD1 could cause ALS.