Type of Document Dissertation Author Rojas, Ana Author's Email Address firstname.lastname@example.org URN etd-08162010-102550 Title A Study of the Elongation of Fibrils of the Alzheimer's Amyloid Beta Protein with a Coarse-Grained Force Field Degree Doctor of Philosophy (Ph.D.) Department Physics & Astronomy Advisory Committee
Advisor Name Title Browne, Dana Committee Chair Kurtz, Richard L. Committee Member Scheraga, Harold A. Committee Member Sprunger, Phillip T. Committee Member Lee, Yong-Hwan Dean's Representative Keywords
- protein folding
- misfolding disease
- molecular dynamics
Date of Defense 2010-07-12 Availability unrestricted AbstractAlzheimer’s disease (AD) is a brain disorder named after the German psychiatrist Alois Alzheimer, who first described the disease in 1906. AD is a form of dementia, characterized by impairment of memory and other intellectual abilities, caused by the loss of neurons and synapses (the structures that permit communication between neurons) in certain regions of the brain. Although the mechanism by which neurons are affected is not yet well understood, research points to a small protein, the beta-amyloid peptide (Abeta), as the first suspect. Ab chains are present in the brains of healthy individuals, but in AD patients, they associate and form clumps that deposit outside neurons, and are believed to trigger the disease.
In this dissertation, I use computational methods to study the behavior of the structures formed by Ab chains, when they associate with each other, and how these structures grow. The goal of this work is to use computational methods to complement
experimental results by filling the gaps about structural and association mechanism that cannot be accessed by experiments.
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