Exploring the Frontiers of Protein Science: Two Inspiring Lectures Delivered by Dr. Yibin Sun and Dr. Rui Lai

“The 21st century is the century of biology.” In recent years, the Nobel Prize in Chemistry has frequently been awarded to biologically-oriented research, reinforcing this statement and highlighting the increasing convergence between chemistry and life sciences. To promote interdisciplinary academic exchange and broaden the horizons of faculty and students, we invited two young scholars—Dr. Yibin Sun and Dr. Rui Lai—to deliver a captivating academic lecture on protein science on May 8, 2025.

Dr. Yibin Sun obtained his bachelor’s degree from Shandong University and his Ph.D. from Xiamen University in 2020. He has since been engaged in postdoctoral research at Peking University. Dr. Sun’s research focuses on catassembly, assembly dynamics, and protein engineering. In his presentation, he introduced ‘catassembly’ as a dynamic process widely present in biological systems, playing a crucial role in biological regulation and functional construction. He elaborated on his team’s innovative work in constructing the first artificial protein catassembly system by rationally designing a fusion protein. Through thermodynamic and kinetic studies, the team revealed the underlying principles and regulatory mechanisms of the system. This achievement not only advances the understanding of catassembly mechanisms in living systems but also provides theoretical foundations for designing artificial assembly systems with tunable rates.

Dr. Rui Lai received his bachelor’s degree from Jilin University and his Ph.D. from the University of Nebraska–Lincoln in 2018. He then conducted postdoctoral research at Boston University and served as an associate researcher at the Dalian Institute of Chemical Physics, Chinese Academy of Sciences. In April 2025, he joined Jilin University. Dr. Lai’s research centers on the development and application of computational methods for biomolecular simulations, with a focus on hybrid quantum mechanics/molecular mechanics (QM/MM) approaches and the design and regulation of enzymatic catalysis. In his talk, Dr. Lai emphasized the importance of artificial enzyme design in modern drug discovery and pointed out the current knowledge gaps in understanding enzyme catalytic efficiency and specificity. He presented a series of recent theoretical advances from his group, including how enzyme active sites stabilize carbene intermediates, the intrinsic mechanisms governing metal ion selectivity in metalloproteins, and the application of multi-scale computational simulations in elucidating the catalytic mechanisms of metalloenzymes—demonstrating the unique value of theoretical calculations in catalysis research.

This academic event provided attendees with a more systematic understanding of protein assembly and enzymatic regulation, sparking greater interest in cutting-edge interdisciplinary topics. The two scholars engaged in in-depth discussions with faculty and students on topics such as the structural tunability of artificial proteins and the selection of computational parameters in simulations. Together, they envisioned the future of chemical biology and the opportunities brought by interdisciplinary integration. The atmosphere was lively and inspiring throughout. We look forward to more such academic exchanges in the future to explore new avenues for chemistry in this era of convergence.

（Drafted by Zhaolin Zhu，reviewed by Guanglu）