Dr. Zhongyu Yang

Associate Professor

Department of Chemical and Biomedical Engineering

University of Missouri, Columbia, MO

Presents via Zoom:

“Confined By Active: From Fundamental Protein Biophysics to Advanced Hybrid Materials”

Friday, March 20th at 12:20 PM

Abbott Hall Room 138

Bio: Dr. Zhongyu Yang earned his bachelor's degree in polymer science and engineering from the University of Science and Technology of China (USTC) in 2004. He then pursued a Ph.D. in physical chemistry at the University of Pittsburgh under Sunil Saxena, specializing in Electron Paramagnetic Resonance (EPR) spectroscopy. In 2010, he moved to UCLA for postdoctoral training with Wayne Hubbell, gaining expertise in biochemistry and biophysics.

In Fall 2015, he began his independent career at North Dakota State University (NDSU), establishing an interdisciplinary research program in biophysics and heterogeneous biocatalysis. Over 8.5 years, he published approximately 85 peer-reviewed articles and 40 conference papers, secured over $6 million in federal and local grants, and mentored nine graduate students, including four Ph.D. recipients, as well as six postdoctoral researchers.

In January 2025, he relocated his research lab to the University of Missouri’s Department of Chemical and Biomedical Engineering. While continuing his work in fundamental protein biophysics, he aims to expand his research into biotic-abiotic interfaces, advancing biomaterials, biocatalysis, sustainable chemistry, and biomedical applications.

Abstract: Proteins are essential for many cellular functions, operating in a highly crowded and confined cellular environment. While most biophysics studies focus on dilute solutions, understanding proteins under native-like conditions is crucial to understanding their biological function and may lead to development of smart hybrid materials inspired by nature. While cellular crowding effect studies have been initiated with promising progress, confinement where proteins are restricted by fixed boundaries remains less understood, due to challenges in mimicking these environments. Our research bridges this gap by investigating protein structure, dynamics, function, translocation, folding, and aggregation within native and synthetic compartments that mimic cellular conditions. Such a cell-free approach not only advances fundamental protein biophysics but also promotes the development of hybrid biomaterials integrating proteins with synthetic components. Our key technical innovation is to use site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy to probe protein structures at the residue level, which overcomes system complexity and heterogeneity and provides otherwise inaccessible structural and dynamic information. This information is also the key to govern the practical performance if hybrid materials based on proteins under confinement are prepared. Our studies span synthetic compartments like polymeric materials, metal-organic frameworks (MOFs), and covalent organic frameworks (COFs), as well as native compartments such as chaperonins and nanopores. We have demonstrated the feasibility of probing these complex protein-compartment systems and extracting valuable insights. In this talk, we will showcase how SDSL-EPR reveals protein-compartment interactions, folding in synthetic environments, translocation into nanoscale channels, and aggregation under confinement. This work will not only enhance our understanding of protein behavior but also promote enzyme-abiotic hybrid material design for biocatalysis, therapeutics, and biomimetic applications.