Dr. Zhu earned his Bachelor`s degree at Nanjing University in 2007 and the PhD degree at Peking University in 2013. As an undergraduate, he joined a research group on membrane chemistry and gained experience on organic synthesis of amphiphilic molecules and IR reflection absorption spectroscopy. At Peking University, he experimentally studied protein folding mechanisms, designed metal binding proteins and protein-protein interactions. He completed the postdoctoral training at Dokholyan lab of UNC Chapel Hill and studied computational protein design. He became the associate professor (tenure-track) at the School of Life Sciences of Tianjin University since 2019. Dr. Zhu`s interdisciplinary research combines biochemistry, biophysics, and computation, for the purpose of designing novel protein structures and functions, including HIV-1 immunogens. His series work of rational protein design was published in Nature Communications, PNAS, Immunity, Structure, Biophysical Journal, Protein Science etc. and highlighted by Science Daily, F1000, and Nature research microbiology community.

Rational protein design provides useful reagents to combat the persistent global threats imposed by rapidly evolving pathogens, such as human immunodeficiency viruse. High accuracy structural design and stabilization of specific conformational states are enabled by advancements in biomolecule modeling, force field development, and sampling methods. As an example of protein design on native conformations, epitope grafting presents the target region on a heterologous protein scaffold with preserved structural or antibody-binding properties. The resulting protein binders and immunogens have the advantages of stability, amenability and selectivity over naturally evolved immunoglobulin or synthesized small molecules.

The goal of Zhu group is to apply computational protein design and biomolecular engineering methods to overcome the barriers to the generation of immunity against foreign antigens (viruses) and mutated self-antigens (cancer antigens). The methods developed in our research enabled atomic-level orchestration of protein conformations and provided valuable reagents for biomedical investigations. We also expand the knowledge of structural design to engineering both native and non-native protein conformers, which are relevant in enzymatic reactions, transformation between active/inactive states, and misfolded proteins in cellular condensates.