Date of Award
5-2024
Document Type
Dissertation
Degree Name
Doctor of Philosophy (PhD)
Department
Physics
Committee Chair/Advisor
Hugo Sanabria
Committee Member
Sapna Sarupria
Committee Member
Feng Ding
Committee Member
Kasra Sardashti
Abstract
Proteins are biomacromolecules responsible for the functions of life. While classically proteins are thought to be well structured in order to perform a specific function, 50% of proteins within Eukaryotic cells contain intrinsically disordered regions (IDRs), regions with no well-defined structure. IDRs are often used for cell signaling, responding to external factors such as temperature changes or the presence of small molecules. To understand how IDRs can function without structure, it is important to understand the dynamics of such systems. Understanding IDR intramolecular and intermolecular interactions will shed light on IDR dynamics. Intramolecular interactions are first explored using fluorescence spectroscopy methods and polymer modeling using the C-terminal domain (CTD) of GluN2B as a sample IDR. Intermolecular interactions are explored using coarse grain simulations to predict biomolecular condensation formation for protein sequences with varying numbers of glutamine. It is found that IDRs show complex dynamics in which secondary structure may play a larger role than previously expected.
Recommended Citation
Latham, Danielle, "Intrinsically Disordered Proteins and Their Role in Biomolecular Condensates" (2024). All Dissertations. 3613.
https://tigerprints.clemson.edu/all_dissertations/3613
Author ORCID Identifier
0000-0003-3964-4228