TSRI Faculty Interests

Molecular Assembly

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.

Bokoch, Gary  
studies the control and integration of cellular activities initiated by GTP-binding proteins, seeking to determine how GTP-binding proteins function, how they are regulated at the molecular level, and how this regulation may be abnormal in various disease states.

Fowler, Velia  
studies the role of actin dynamics in regulating assembly and function of cytoskeletal structures that contribute to cell and tissue morphogenesis during embryonic development. Systems of interest include morphogenesis of epithelia, the eye lens, differentiation and stability of erythrocytes, and striated muscle development.

Gerace, Larry  
seeks to understand the mechanisms for regulation of signaling and cell differentiation by components of the nuclear envelope, particularly in regard to muscle, and the machinery for posttranscriptional regulation of gene expression by nucleocytoplasmic transport, mRNA translation and protein turnover, with focus on HIV-1.

Ghadiri, M.Reza  
develops novel methods for the rational design and construction of functional and interesting bioorganic molecules, such as novel antimicrobial agents, catalytic peptides, biosensors, self-replicating systems, and molecular logic gates.

Millar, David  
uses single-molecule fluorescence and time-resolved laser spectroscopy to study the dynamics of enzyme-DNA interactions and the folding of catalytic RNA molecules.

Milligan, Ronald  
uses cryo-electron microscopy and image analysis to study the structure and mechanism of action of large molecular machines such as actomyosin, kinesin-microtubules, MAPs-microtubles, VCP/p97 and dynein AAA ATPases, various membrane channels and transporters, and bacterial toxins.

Nicolaou, K.C.  
works on the total synthesis of biologically active natural and designed molecules and the discovery and development of new synthetic strategies and technologies.

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

Rebek Jr., Julius  
studies basic questions of molecular recognition, self-assembly, catalysis, and complementarity by designing novel organic molecular nanocapsules and synthetic receptors.

Stout, C. David 
determines crystal structures of a variety of biological macromolecules, primarily integral membrane associated enzymes and proton pumps, cytochrome P450s, and iron-sulfur enzymes, and including HIV protease mutants, self-assembling peptides, and RNA-protein complexes, in order to understand structure-function relationships and establish mechanism.

Tainer, John  
develops and applies advanced tools for high-impact structural biology including combined x-ray scattering in solution and x-ray crystallography on complexes at his synchrotron beamline to bridge from complexes and conformations to pathways and phenotypes by characterizing macromolecular machines, novel inhibitors, and the molecular basis for diseases and intervention strategies.

Williamson, Jamie  
studies the structure and dynamics of RNA molecules and RNA-protein complexes involved in the regulation of gene expression by employing NMR spectroscopy and X-ray crystallography for solving high-resolution three-dimensional structures and examining the mechanism of assembly of multiprotein-RNA complexes.

Wilson, Ian  
has broad structural biology and structural genomics programs to determine thee-dimensional structure and biological function in a number of systems related to humoral, cellular and innate immunity, human disease, drug and vaccine design, influenza virus, HIV-1 , the expanding protein universe and metagenomics.