Date of Award
1-1-2019
Language
English
Document Type
Dissertation
Degree Name
Doctor of Philosophy (PhD)
College/School/Department
Department of Chemistry
Content Description
1 online resource (xiii, 117 pages) : color illustrations.
Dissertation/Thesis Chair
Jayanti Pande
Committee Members
Jayanti Pande, Alexander Shekhtman, Li Niu, John Welch, Chunyu Wang
Keywords
alpha-crystallin, chaperone, lens, melittin, NMR, substrate, Crystalline lens, Cataract, Molecular chaperones
Subject Categories
Chemistry
Abstract
The α-crystallins (αA- and αB-crystallin isoforms) from the ocular lens are small heat shock proteins and molecular chaperones, widely believed to play a significant role in protecting the lens from cataract. Mutations and modifications on human αA- and αB-crystallin (HAA and HAB, respectively) are linked to a variety of diseases, including cataract formation, neuropathological protein folding disorders, and many others. It is believed that HAA and HAB prevent the aggregation of other lens proteins. However, the structural and thermodynamic details of the chaperone-substrate (aka “client”) interaction are sparse. Therefore, the main objective of this dissertation is to reveal structural and thermodynamic aspects of such interaction, using a model substrate, the 26-residue peptide melittin.
Recommended Citation
Ramirez, Lisa Marie S., "Modeling chaperone-substrate interactions of alpha crystallin from the ocular lens" (2019). Legacy Theses & Dissertations (2009 - 2024). 2366.
https://scholarsarchive.library.albany.edu/legacy-etd/2366