Ubiquitin ERNST ensemble · PDB 2KOX ↗ · motion interpolated between ensemble members
Exploring molecular life. Connecting disciplines.
BioNMR LabDonghan Lee’s Research Group
KBSIKorea Basic Science Institute
USTUniversity of Science & Technology
Structure. Dynamics. Function.
Our research
Beyond a static picture.
Proteins move. They change shape, recognize partners, and carry signals. We study the motions that make biology work.
01 / METHODS
Making the invisible visible.
Advanced NMR methods and deep learning bring transient protein states into focus.
Explore NMR & AI
We develop CPMG and R₁ρ relaxation-dispersion methods to probe microsecond-to-millisecond dynamics, including the supra-τc window. Deep learning helps make the analysis of time-domain NMR signals more robust.
From disordered proteins to allostery, we connect molecular motion with biological function.
Explore protein dynamics
We investigate p53 and 4EBP1, the collective motions of ubiquitin, and allosteric communication in proteins such as guanylate kinase. Our goal is to understand how conformational ensembles shape molecular recognition.
NMR-guided screening and structural insights help us investigate therapeutic targets.
Explore drug discovery
Our work includes BLVRB inhibitors, drug repositioning for PTP4A3 (PRL-3), and the p53–MdmX/Mdm2 interaction. We connect computational screening with experimental investigation.