Danny’s research focuses on atomic and molecular insights into the structure-function relationships (SARs) of biomolecules. Danny coined the term "pyrophosphate cage", to describe how the potent antimicrobial peptide, Nisin, recognizes bacterial cell wall precursor, Lipid II, to achieve the novel targeted pore-forming bactericidal activity. He reported the first demonstration of direct structural investigation of the dynamic co-translational folding events of a nascent polypeptide chain as it emerges from the ribosome by using NMR, which has paved the way towards fundamental understanding of protein folding and misfolding. He also unravelled unique structural and dynamic features of several oncogenic DNA/RNA G-quadruplex forming motifs to help drug designs. After starting his independent career in Taiwan, Danny continues to deepen our basic understanding of protein folding (particularly the folding of topologically knotted proteins) while collaborating with several research teams to study novel lectins and glyco/membrane proteins. His recent research focuses on the SARs of post-translationally modified proteins in the context of glycosylation and ubiquitination. To address these issues, he has employed an integrated approach using cryo-electron microscopy, X-ray crystallography, NMR spectroscopy, mass spectrometry, small angle X-ray scattering and atomic force microscopy to glean multi-scale structural information.