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Engineering Protein Function Through Directed Evolution
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Fu-Cheng Liang

Fu-Cheng Liang

Midwestern State University, Texas

Dr. Fu-Cheng Liang serves as an Associate Professor of Biochemistry within the Department of Chemistry at Midwestern State University (MSU). At the forefront of his academic pursuits, Dr. Liang's research laboratory is dedicated to the exploration of protein biochemistry, with a particular emphasis on protein targeting and translocation in bacteria and chloroplast. Notably, his research interests have expanded to encompass the study of protein aggregation-prone diseases, including Alzheimer's and Parkinson's disease. Dr. Liang earned his Bachelor of Science in Chemistry from National Chung Cheng University in Taiwan, followed by a Master of Science in Chemistry from National Taiwan University. He furthered his academic journey by obtaining a Ph.D. in Medical Science from Texas A&M Health Science Center. During his doctoral studies, Dr. Fu-Cheng developed a cutting-edge fluorescence-based protein translocation assay, contributing significantly to unraveling the intricate mechanisms governing protein transport across bacterial cellular membranes. Continuing his commitment to advancing scientific knowledge, Dr. Fu-Cheng embarked on postdoctoral training in the Division of Chemistry and Chemical Engineering at the prestigious California Institute of Technology. There, he utilized state-of-the-art NMR spectroscopy techniques to investigate how membrane protein chaperones employ spatiotemporal regulation to prevent substrate aggregation during the complex process of membrane protein biogenesis. 

Collection Overview

Managing protein homeostasis is imperative for the normal functioning of cells, necessitating precise control over protein folding, localization, and interactions. Dysregulation in these processes, such as protein misfolding and aggregation, has been implicated in various protein aggregation-prone diseases. The optimization of protein folding in vivo presents a promising avenue for reshaping protein function and enhancing the production of desired proteins. Direct evolution is one of the most effective and specific methodologies for achieving this optimization.  

Directed evolution expedites the natural selection of protein variants by subjecting them to multiple iterative rounds of library screening. This approach proves invaluable in identifying proteins with improved folding and enhanced functional properties. It has evolved into a powerful and widely adopted tool, capable of engineering superior or novel functions in proteins, metabolic pathways, and even entire genomes.  

This comprehensive collection aims to explore the diverse directed evolution methods employed for screening protein variants. Doing so provides a nuanced understanding of the intricacies involved in optimizing protein folding and reengineering protein function. Through a detailed exploration of these methodologies, this collection aims to contribute valuable insights into the broader landscape of protein engineering, offering a deeper appreciation for the potential applications and advancements in this evolving field. 

Articles

Optimized Yeast Surface Display Workflow for Directed Evolution of Proteases

Optimized Yeast Surface Display Workflow for Directed Evolution of Proteases

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2026

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