TSRI Faculty Interests

Structural Biology

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.

Carragher, Bridget  
is developing, testing, and applying technology for specimen handling, automated acquisition, automated processing, and information handling in electron microscopy; one of the goals is to completely automate cryo-electron microscopy in order to solve macromolecular structures.

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.

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.

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.

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.

Ollmann Saphire, Erica  
combines x-ray crystallography, biochemistry, and immunology to analyse proteins that play key roles in the pathogenesis of Ebola and other viral hemorrhagic fevers; structures of these proteins provide templates for vaccine design and enable rapid responses to newly emerging forms of the viruses.

Otomo, Takanori  
studies structure and function of proteins involved in the autophagic pathway.

Schork, Nicholas  
focuses on the development and implementation of analysis methods for understanding the genetic determinants of complex human traits and diseases such as cancer, neuropsychiatric disease, and cardiovascular disease. These methods focus on both the design, integration, and interpretation of studies making use of contemporary high throughput genomic technologies.

Stevens, Raymond  
uses crystallography and biochemistry to probe the structure and function of molecules involved in neurotransmission and neurochemistry, seeking to understand how neuronal cells communicate at the molecular level and to create new molecules that affect neuronal signal transduction and recognition.

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.

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.

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.

Wuthrich, Kurt  
develops advanced techniques in nuclear magnetic resonance (NMR) spectroscopy and applies them in protein structural biology and structural genomics projects.