Date of Last Revision

2015-06-17 11:17:40


Chemical Engineering - Cooperative Education

Degree Name

Bachelor of Science

Date of Expected Graduation

Spring 2015


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.

Research Sponsor

Jie Zheng

First Reader

Dr. Edward Evans

Second Reader

Dr. Richard Elliott



To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.