Wen Zhu
Florida State University, FL·Biochemistry
Enzymes are proteins that speed up chemical reactions, and they do not hold still. They flex and shift between shapes, and these motions matter for how well they work.
- Fields
Biochemistry
Biophysics
Chemistry
- Topics
enzyme dynamics
conformational dynamics
asparagine synthetase
- Grants
- 1 known grant, through Aug 2030
What they work on
- Test whether mutations far from the active site impair asparagine synthetase (ASNS) by altering its protein motions, comparing normal enzyme with two variants linked to asparagine synthetase deficiency.
- Quantify differences in protein flexibility between normal and mutant ASNS using time- and temperature-dependent HDX-MS, a method that tracks how quickly the protein exchanges hydrogen for deuterium.
- Measure how disease variants change individual steps of the ASNS reaction using enzyme kinetics, and link these changes to the measured dynamics.
- Examine how networks of hydrophobic amino acids transmit the effects of distant mutations, using a cell-based functional complementation assay that tests whether variants restore enzyme function.
More about the research
Many inherited diseases are caused by missense mutations, single changes in a protein's building blocks. Some of these changes sit far from the enzyme's active site, the pocket where the reaction happens, yet they still impair function. The project proposes that such distant mutations work by changing the enzyme's motions.
Why it matters
Many inherited diseases come from enzyme mutations whose harm is hard to explain from structure alone. Linking those mutations to altered protein motion could help explain disorders like asparagine synthetase deficiency. In the future, this understanding could inform new ways to adjust the activity of faulty disease-associated enzymes.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Raquel Lieberman
Georgia Institute of Technology, GA·Biochemistry
Screen the baker's yeast gene-deletion library for strains that survive toxic mutant myocilin, to find cellular pathways that make cells vulnerable to this glaucoma protein.
Rovshan Sadygov
University of Texas Medical Branch at Galveston, TX·Biochemistry
Develop methods to estimate protein turnover from the deuterium labeling of fragment ions in tandem mass spectra, which are less distorted by space-charging, limited dynamic range and co-eluting contaminants than intact peptide ions.
Sefika Ozkan
Arizona State University Campus Immersion, AZ·Biophysics
Develop models that predict how much binding affinity changes when amino acids far from a protein's binding site are substituted, using molecular dynamics and force perturbation on the E. coli lactose repressor (LacI).
The school
Florida State University: 15 labs on PI Pages, $461M a year on research, 481 research doctorates a year.
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