The relationship between the structure and function of proteins is a fundamental problem in biology with implications for the future of biotechnology and global health. For example, changes to the structure of a coronavirus spike protein led to a global pandemic where our best defenses were vaccines that could only be designed with an intricate knowledge of the virus's structure. Proteins, such as those that comprise a virus's shell, are often thought of as completely distinct from synthetic polymers, due to their rigid, folded structure. However, unfolded, intrinsically disordered proteins and proteins with unfolded domains known as intrinsically disordered regions show semi-flexible polymer behavior, challenging this classification. Thus, it is necessary to understand the function of amino acid sequences that lack structure, such as the intrinsically disordered proteins found in membraneless organelles, which are involved in spatiotemporal control of cell metabolism. This dissertation will investigate how the properties of macromolecular assemblies are determined by the structural properties of their components both biological and synthetic. It includes collaborations with experimentalists, which show how these properties impact material function in applications where species are compartmentalized including water filtration, plastic upcycling, gene therapy, and bio-nanoreactors.

Creator

• Waltmann, Curt

DOI

• https://doi.org/10.21985/n2-rg6b-vp09

Subject

• Materials Science

Language

• en

Alternate Identifier

• http://dissertations.umi.com/northwestern:16624
• etdadmin_upload_991536

Date created

• 2023-01-01

Resource type

• Dissertation

Rights statement

• In Copyright