The Pielak Group
My students and I use the formalisms of equilibrium thermodynamics and the tools of molecular biology and biophysics to understand the structure, stability, and function of globular and intrinsically-disordered proteins in physiologically relevant environments.
This method allows us to obtain high resolution NMR data from proteins in living cells. This work involves quantifying the effects of macromolecular crowding on protein stability, structure, dynamics and protein-protein interactions.
We are exploring the effects of macromolecular crowding on protein stability, dynamics and structure in vitro using both synthetic polymers and proteins as crowding agents.
Tardigrades, commonly known as water bears, are microorganisms that can survive extreme conditions including a decade of dehydration. We are studying the proteins that allow these hardy creatures to survive this condition.
19F, 1H, 15N, and 13C High Res Protein NMR
NMR in Bacterial Cells and Oocytes
Circular Dichroism Spectropolarimetry
Fourier Transfer Infrared Spectroscopy
Differential Scanning Calorimetry
Isothermal Titration Calorimetry
Pressure Perturbation Calorimetry
Escherichia coli Molecular Biology
Protein Expression and Purification