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TSRI Faculty Interests
Biophysics Asturias, Francisco
studies the structures of macromolecular assemblies involved in eukaryotic gene expression and its control, such as complexes formed by RNA polymerase II and general transcription factors, using the technique of cryoelectron microscopy.
Chang, Geoffrey
is interested in the structural basis of the transport of substrate across the cell membrane by ion channels and transporters; he determines the structures of such integral membrane proteins through high-resolution x-ray crystallography.
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.
Getzoff, Elizabeth
aims to characterize functionally important protein conformational states by coupling crystallography, spectroscopy, molecular biology and computational analyses, and to apply that knowledge to protein and inhibitor design for key biological processes, including photoactivity, electron transfer, and enzyme catalysis.
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.
Goodin, David
is focused on the rational engineering of metalloenzyme catalysts in order to better understand the chemical diversity of natural enzymes and to generate novel catalysts of potential utility.
Jegla, Timothy
aims to define the molecular pathways through which potassium channels regulate neuronal signaling.
Johnson Jr., John
uses a variety of cellular and molecular biology methods to develop and test atomic resolution models of particle-related events in the virus life cycle; he also uses viruses as a paradigm for developing methods to determine atomic resolution models of cellular mega-structures.
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.
MacRae, Ian
combines structural biology, biochemistry and cell biology to understand mechanisms of gene regulation by RNA interference.
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.
Noodleman, Louis
uses quantum chemistry and protein electrostatics to investigate the electronic structures and active site mechanisms of redox metalloproteins, such as respiratory iron-sulfur proteins, the nitrogen fixing nitrogenase enzyme, and the iron-oxo dimer enzymes methane monooxygenase and ribonucleotide reductase.
Otomo, Takanori
studies structure and function of proteins involved in the autophagic pathway.
Powers, Evan
is interested in the energetics and mechanisms of protein folding and aggregation.
Romesberg, Floyd
seeks to understand and evolve novel protein function by expanding the genetic code, to understand the molecular basis of DNA damage, repair, and mutagenesis, and to use femtosecond laser pulses to probe protein dynamics.
Schmid, Sandra
is defining the molecular mechanisms of receptor-mediated endocytosis, which involves the concentration of receptor-ligand complexes into clathrin coated pits, their internalization via coated vesicles, and the regulation of these events by GTPases and kinases.
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.
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.
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