Thomas Szyperski
University at Buffalo, NY·Biophysics
A protein's job depends on the 3D shape its chain folds into, and that shape shifts with temperature and pressure. Little is known about the shapes proteins adopt in extreme cold or at pressures of hundreds of atmospheres.
- Fields
Biophysics
Biochemistry
Chemistry
- Topics
protein folding
cold denaturation
cold unfolding proteins
- Grants
- 1 known grant, through Jul 2027
What they work on
- Test whether a protein core mixing hydrophobic (water-avoiding) and hydrophilic (water-loving) parts yields a partly cold-unfolded state that includes water, using computationally designed proteins, biophysical measurements and molecular dynamics simulations.
- Characterize energy landscapes, thermodynamic signatures and pressure–temperature phase diagrams of designed cold unfolding proteins, testing whether cold-state cooperativity drops as the core becomes more hydrophilic.
- Develop computational design protocols for beta-sheet cold unfolding proteins, and redesign natural proteins to unfold under extreme conditions, to validate the new folding principles.
More about the research
Yet these conditions are common in oceans and polar regions, and they also matter for vaccine and protein-drug formulation. This collaborative project, shared with Dr. Kuhlman, studies "cold unfolding proteins," which lose their defined shape when chilled. The goal is rules that predict protein shapes and energies under extreme conditions.
Why it matters
Predicting how proteins behave in cold and high-pressure conditions could help explain life in deep oceans and polar regions. It could also improve how protein drugs and vaccines are formulated and stored, and help engineer cold-adapted proteins for biotechnology. The design tools and software will be shared with other researchers.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Brian Kuhlman
University of North Carolina at Chapel Hill, NC·Biochemistry
Test whether a protein core mixing water-repelling and water-attracting amino acids yields a partly unfolded, water-containing cold state, using de novo designed cold unfolding proteins, biophysical measurements and molecular dynamics simulations.
Ronald Levy
Temple University, PA·Biophysics
Determine the physical basis of epistasis, where one mutation's effect depends on others, in HIV integrase and capsid under different drugs, using molecular dynamics simulations and virus data to build drug-specific fitness landscapes.
Alberto Perez
University of Florida, FL·Biophysics
Map the binding partners of the ET domain of BET proteins: identify candidates computationally, rank the strongest with machine learning and physics-based methods, and check top leads with NMR experiments.
The school
University at Buffalo: 32 labs on PI Pages, $542M a year on research, 316 research doctorates a year.
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