Decoding the Structural Response of Disordered Proteins to their Surrounding Environments
Abstract
This dissertation examines how the sequence and the chemical environment of intrinsically disordered protein regions (IDRs) affect their structure. Unlike structured proteins, IDRs do not adopt a singular structure. Instead, they exist in a dynamic conformational ensemble. The conformations that make up this ensemble are shaped by a range of molecular interactions, both with the environment and within the IDR itself. The absence of a stable three-dimensional structure, along with their high level of exposure to the solvent environment, makes IDR exceptionally adaptable to changes in their physical and chemical surroundings. My research employs computational methods to investigate how IDRs respond to different chemical environments and physical constraints. I will discuss how we quantify the contribution of IDR structural preferences to their entropic forces and describe how we leverage IDR sensitivity to design biosensors.