BIOLOGICAL CHEMISTRY Protein-Mediated Molecular Recognition  UNC Chemistry
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Methods

Analytical Ultracentrifugation

Circular Dichroism Spectropolarimetry

Differential Scanning Calorimetry

Isothermal Titration Calorimetry

Multidimensional Protein NMR

Site-Directed, Random-Mutagenesis

Site-Directed, Combinatorial-Mutagenesis

Pressure Perturbation Calorimetry

Synopsis Present Research at UNC

My students and I use the formalisms of equilibrium thermodynamics and the tools of molecular biology and biophysics to understand protein structure, stability, and function. Currently, our research focuses on three topics.

1. In-cell NMR. This new 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, dynamics and structure.

2. 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.

3. We are studying the oxidative aggregation of the key protein involved in Parkinson's disease, alpha-synuclein.Endeavors

Gary J. Pielak, CB# 3290, Venable and Kenan Laboratories, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-3290, 919-966-3671