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Cheng Hui-Chun’s Groundbreaking Research on the Dynein Motor Domain
Dr. Cheng Hui-Chun, an assistant professor at the Institute of Bioinformatics and Structural Biology at NTHU, has recently had her paper titled “Allosteric Communication in the Dynein Motor Domain” published in the prestigious journal Cell. Her groundbreaking research focuses on how dynein ATPases control structural change and how dynein controls the ATP hydrolysis environment. Cheng’s findings promise to extend our understanding of the nerve degeneration characteristic of such conditions as Alzheimer’s disease and Parkinson’s disease.
 
In the paper Dr. Cheng states that the molecular motor consists of a group of proteins with a very interesting function and structure, and that it plays many important roles in the cell, such as DNA replication, protein synthesis and degradation, energy generation, mass transport, and flagella and cilia oscillation. As one of these molecular motors, dynein is responsible for transporting both waste and useful substances—two processes essential to maintaining the body’s functions. Comparing human cells to a city, she likens dynein to trucks responsible for transporting essential materials.
 
In recent years, molecular motors have become a hot research topic. While the mechanisms by which many molecular motors function have been solved, dynein remains an exception. Although dynein was discovered back in the 1960s, we still have a rather limited knowledge of its mechanism of action. This is mainly due to dynein’s very high molecular weight, making it difficult to carry out purification and further quantitative analysis.
 
However, Dr. Cheng came up with a way to overcome the problems of purification and crystallization. Simplifying the procedure by using the techniques of protein engineering, she managed to cut the dynein, leaving only the core part, to increase the yield of the protein and enhance the success of its crystalization rate. In addition to addressing the problem of purification, Cheng used X-ray diffraction to obtain the three-dimensional structure of dynein. Working together with Dr. Gira Bhabha of the University of California, San Francisco, she used a cryo-electron microscope to discover a number of dynein’s movement mechanisms, including its structure in a three-dimensional space, and how it changes shape when transporting substances. These discoveries are highly significant, for this is the first time researchers have gained in-depth information on the mechanism underlying the movement of dynein.
 
Dr. Cheng says that from the perspective of basic scientific research, it is important to increase our understanding of the mechanism underlying the structural changes of dynein, since doing so increases our understanding of the molecular motor. In medicine, dynein has been implicated in many neurodegenerative diseases, such as Parkinson 's disease, Huntington's disease, and Alzheimer's disease. Research on dynein will have a key role to play in the development of drugs for treating these diseases by either speeding up or slowing down molecular motion.
 
 The structural change of dynein and the catalytic cycle of ATPases.

The structural change of dynein and the catalytic cycle of ATPases.

Professor Cheng Hui-Chun of NTHU’s Institute of Bioinformatics and Structural Biology.

Professor Cheng Hui-Chun of NTHU’s Institute of Bioinformatics and Structural Biology.

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