Dr. Danny Hsu is a Research Fellow at the Institute of Biological Chemistry, Academia Sinica. During his doctorate study at Utrecht University, the Netherlands, he determined the atomic structure of a lantibiotic, nisin, in complex with Gram-positive bacterial cell wall precursor, Lipid II. He coined the term "pyrophosphate case" to explain how nisin targets Lipid II to achieve its antimicrobial activity, providing a blueprint for future antibiotics developments. During his postdoctoral research at the University of Cambridge, UK, Danny demonstrated the proof of concept of using solution-state NMR spectroscopy to investigate the co-translational folding of nascent polypeptide chains on the ribosome. His earlier independent research focused on the folding mechanisms and functional implications of topologically knotted proteins. He currently focuses on developing an integrated biophysics and structural biology platform, including cryo-electron microscopy, mass spectrometry, and molecular modeling, to investigate the structure-activity relationship (SAR) of glycoproteins, and coronavirus spike proteins, in particular, and how mutations impact on the SAR in the context of glycosylation.
