TSRI Faculty Interests

Protein Folding

Balch, William E. 
is interested in the biochemical and molecular basis for vesicular trafficking from the endoplasmic reticulum to the cell surface, particularly in the structures, functions, and mechanisms of control exerted by small GTP-binding proteins.

Dawson, Philip  
develops novel chemical ligation methodologies for the synthesis of natural and chemically engineered proteins to develop novel peptide based vaccines for HIV-1, study the molecular basis of protein folding and enzymatic catalysis, conjugate biological macromolecules to in complex systems such as cells, viruses and Quantum Dots and to develop synthetic protein pharmaceuticals.

Deniz, Ashok  
develops and uses single-molecule fluorescence methods to study the dynamics and interactions of biological molecules during such processes as protein/RNA folding and assembly of the 30S subunit of the bacterial ribosome.

Dyson, Helen Jane  
uses NMR to study the protein-folding process and to study the nature and behavior of unfolded and partly folded forms of proteins, including prion proteins and several newly-discovered, intrinsically unstructured proteins.

Kelly, Jeffery  
examines the bioorganic and biophysical chemistry of aberrant conformational changes in proteins associated with misfolding diseases, seeking to develop new approaches for preventing these diseases with purposefully designed small molecules.

Powers, Evan  
is interested in the energetics and mechanisms of protein folding and aggregation.

Wiseman, R. Luke  
is interested in understanding the cellular and energetic factors that dictate intracellular protein folding as it relates to human disease.

Wright, Peter  
uses high-resolution, multi-dimensional, hetero-nuclear magnetic resonance (NMR) spectroscopy to study protein dynamics, folding, and recognition, particularly of structures of protein-DNA and protein-protein complexes involved in the regulation of transcription.