Ph.D.

Professor

Biochemistry - CAFNR

Dynamic biological assemblies are strategic and fascinating. We have been exploring molecular recognition by flexible proteins and automatic tracking of changes in complex spectra and medical images.

Molecular recognition by proteins with intrinsic disorder

A pivotal virus-membrane interaction: Coronaviruses use a region of Spike to merge the viral envelope with the host cell membrane. We continue to be interested in the nature of the lipid interactions with this fusogenic region of Spike. Our articles reported (i) the NMR structure of the fusion peptide in a simple membrane-mimicking environment and (ii) its insertion and distortion of the simple membrane mimic via NMR-guided molecular dynamics simulations.

Control point of biosynthesis of oils in chloroplasts: The making of plant oils, e.g. in soy and canola, begins with the highly regulated first step of fatty acid biosynthesis. This is the conversion of acetyl-CoA to malonyl-CoA by acetyl-CoA carboxylase (ACCase). Some of the numerous subunits of the ACCase in chloroplasts may regulate the flow of carbon into oil biosynthesis. We are interested in the assembly of the subunits, their intrinsically disordered parts, and relevance to the regulation. We reported evidence of pH-sensing by BADC and BCCP subunits, with potential to regulate the biotin carboxylase activity during the daily light-dark cycle.

Taking Signal Tracking to Heart

We developed an automatic way to resolve many kinds of change from series of complicated spectra or images, e.g., changes like ligand binding, protein unfolding, and heartbeat. We have developed software approaches that include applications to NMR-based drug screening, mitigation of breathing motion in free-breathing cardiac MRI, and characterization of irregular heartbeats in real-time MRI.

Educational background

• Ph.D. Biophysics, University of Illinois Urbana-Champaign
• B.S. Biochemistry/Computer Science, Oklahoma State University