Date of Graduation

Spring 2015

Document Type

Honors Research Project

Degree Name

Bachelor of Science

Major

Chemical Engineering - Cooperative Education

Research Sponsor

Jie Zheng

First Reader

Dr. Edward Evans

Second Reader

Dr. Richard Elliott

Abstract

In order to discover the most significant residues involved in hIAPP fibril formation, Replica Exchange Molecular Dynamics (REMD) trajectories of both fibril forming hIAPP dimers and non-fibril-forming rIAPP dimers were analyzed. An import heuristic for this is the minimum distance between the peptides. To gain a greater resolution than the standard center of mass distance or 1-1, 2-2, etc.\ residue distances, every permutation of residue distance between molecules of the dimer was measured ranked. It was found that while the rIAPP had a single favored contact, (26 10), hIAPP appeared to have a network of at least three significant contacts: (25 18), (33 11), and (29 22). This network appears to play a part in hIAPP's propensity for fibril formation, and should be the target of mutation simulation.

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