Date of Last Revision
2023-05-02 14:20:24
Major
Chemical Engineering - Cooperative Education
Degree Name
Bachelor of Science
Date of Expected Graduation
Spring 2015
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.
Research Sponsor
Jie Zheng
First Reader
Dr. Edward Evans
Second Reader
Dr. Richard Elliott
Recommended Citation
Kohler, Zak, "Predicting Key Residues Relevant to hIAPP Fibril Stability Using Permuted Residue Minimal Distance Pairs of rIAPP and hIAPP Dimers" (2015). Williams Honors College, Honors Research Projects. 185.
https://ideaexchange.uakron.edu/honors_research_projects/185
hiapp_hiapp_nearest_freq_2of3.png (56 kB)
hiapp_hiapp_nearest_freq_3of3.png (54 kB)
hiapp_hiapp_nearest_freq_allof3.png (52 kB)
hiapp_hiapp_closest_residues_residue_time.png (27 kB)
riapp_riapp_nearest_freq_1of3.png (56 kB)
riapp_riapp_nearest_freq_2of3.png (55 kB)
riapp_riapp_nearest_freq_3of3.png (53 kB)
riapp_riapp_nearest_freq_3of3.png (53 kB)
riapp_riapp_nearest_freq_allof3.png (51 kB)
riapp_riapp_closest_residues_residue_time.png (28 kB)
hiapp_hiapp_secondary_downsampled.png (25 kB)
riapp_riapp_secondary_downsampled.png (25 kB)
hIAPP_vs_rIAPP_secondary.png (20 kB)
hiapp_hiapp_closest_residues_residue.gif (3825 kB)