| Start Date: | 6/3/2014 | Start Time: | 10:00 AM |
| End Date: | 6/3/2014 | End Time: | 11:00 AM |
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Event Description
Micholas Smith,
doctoral candidate, Department of Physics, Drexel University
Influence of Aqueous-Salt Conditions on the Structure and Dynamics of the Monomeric and Novel Dimeric Forms of the Alzheimer's Aβ21-30 Protein Fragment
The behavior of the Alzheimer's related peptide Aβ is the subject of much study. In typical computational studies the environment local to the peptide is assumed to be pure water; however, in vivo the peptide is found in the extracellular space near the plasma membrane which is rich in ionic species. In this thesis the structure and dynamics of a small folding nucleus of the Aβ peptide (Aβ21-30) is examined under a variety of ionic environments. Further, study of mutations of this region are also studied under aqueous salt-environments to elucidate details of how aqueous salts modify the region's behavior. Additionally, as experimental results have highlight that aggregation rates of the full-length peptide are modified by the presence of CaCl2, this work also examines novel dimers states of Aβ21-30 and their stability when exposed to CaCl2.
Advisor: Professor Luis R. Cruz Cruz |
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Location:
Bossone Research Center, Mitchell Auditorium, 3140 Market Street, Philadelphia, PA 19104 |
Audience:
Current StudentsFaculty |
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