Protein Structure and Folding

Berghuis, Albert M.

Berghuis, Albert M., Professor and Chair
albert.berghuis [at]
Structural biological studies of proteins, particularly bacterial enzymes responsible for antibiotic resistance and enzymes that can be exploited as novel targets for antibiotics and antimycotics. Furthermore, efforts are ongoing to exploit the three-dimensional structural information obtained for the structure-based design of novel antimicrobial agents, using computational methods.

Gehring, Kalle

Gehring, Kalle, Professor
kalle.gehring [at]
Structural biology and biophysics of proteins and nucleic acids. The laboratory’s main research interests are poly(A) binding protein, ubiquitin-associated proteins, proteins involved in membrane trafficking, and ER protein folding. The methods used are nuclear magnetic resonance spectroscopy, X-ray crystallography and small-angle X-ray scattering in combination with the techniques of molecular biology.

Gros, Philippe

Gros, Philippe, Professor
philippe.gros [at]
Our laboratory uses a genetic approach in mouse to discover genes, proteins and pathways that play an important role in complex human diseases. Our long-term objectives are to translate knowledge obtained in laboratory mouse models, into clinical outcomes through the creation of novel diagnostic tools or new small molecules modulators with therapeutic value in the corresponding human disease. We are currently focusing on three major human diseases known to have clear genetic component: infectious diseases, cancer, and the birth defect spina bifida. Our genetic platform is based on the use of genetically diverse mouse inbred strains, recombinant congenic strains, and experimentally induced mutagenized mouse stocks (ENU mutants).

Guarne, Alba

Guarne, Alba, Professor
guarnea [at]
Our goal is to understand how proteins determine the fate of DNA during chromosome replication and repair. In particular, how regulatory proteins orchestrate the stabilization of damaged replication forks with DNA repair and forks restart. Since most of the proteins that regulate these processes lack a measurable enzymatic activity, our efforts are aimed at seeing how they work using a broad range of structural biology techniques. We then combine structural information with biochemical and genetic analysis to elucidate their functions at a molecular level.

Huang, Sidong

Huang, Sidong, Assistant Professor
sidong.huang [at]
Our laboratory uses functional genomic tools to study cancer-relevant pathways and to guide targeted cancer therapy. We aim to identify novel genes and networks that modulate response to cancer drugs, and to uncover genetic dependencies between the major signaling pathways in cancer that can be exploited therapeutically.

Nagar, Bhushan

Nagar, Bhushan, Professor
bhushan.nagar [at]
X-ray crystallography, NMR, SAXS and biophysical characterization of proteins in cellular signal transduction pathways that control innate immunity, protein translation initiation and RNA interference with emphasis on molecular mechanisms of regulation. Structural information will be used to glean protein function and aid in the rational development of therapies against cancer and diseases associated with infection and autoimmunity.

Pause, Arnim

Pause, Arnim, Professor
arnim.pause [at]
(1) Molecular characterization of the von Hippel-Lindau (VHL) tumor suppressor gene pathway, identification of new targets of the VHL ubiquitin ligase, mechanism of tumorigenesis in VHL tumors (renal cell carcinoma) and C.elegans, development of animal models of kidney cancer (mice and C.elegans). (2) Functional characterization of the Birt-Hogge-Dube (BHD) tumor suppressor protein in kidney cancer and in cellular and whole animal metabolism (mice and C.elegans). (3) Functional characterization of a tyrosine phosphatase involved in tumor suppression, studies in cellular and animal models.

Pelletier, Jerry

Pelletier, Jerry, Professor
jerry.pelletier [at]
Chemical Biology Approach to Study Regulation of Eukaryotic Translation — Chemical Biology Approach to Interdict miRNA—mediated Repression — Targeting Translation Initiation in Cancer as a Therapeutic Avenue — Use of Mechanism Based Mouse Models to Study Response to Chemotherapy — Biology of RNA Helicases.

Schmeing, Martin

Schmeing, Martin, Associate Professor
martin.schmeing [at]
The Schmeing lab combines X-ray crystallography, electron microscopy and biochemical techniques to study large macromolecular machines that perform important cellular processes. Of particular interest is the ribosome, which synthesizes all proteins, and nonribosomal peptide synthetases (NRPSs) a class of megaenzymes which produce a large variety of small molecules with important and diverse biological activity. For example, NRPSs synthesize anti-fungals, anti-bacterials, anti-virals, anti-tumourigenics, and immunosuppressants including well-known compounds such as penicillin and cyclosporin.

Sonenberg, Nahum

Sonenberg, Nahum, Professor
nahum.sonenberg [at]
Control of translation in eukaryotes; translational control cancer, obesity and neurodegenerative diseases; translational control of learning and memory; ‘knock-out’ mice in translation initiation factors.

Thomas, David Y

Thomas, David Y., Professor
david.thomas [at]
There are two major projects in this group. Cell signaling pathways and molecular chaperone systems in the endoplasmic reticulum and their role in diseases. We use a variety of genetic, biochemical informatics and structural approaches to these problems.

Young, Jason C

Young, Jason C., Associate Professor
jason.young2 [at]
In cells, the folding of polypeptides into mature proteins depends on a specialized class of proteins termed ‘molecular chaperones’, which also protect against potentially toxic polypeptide aggregation. Two of the most important cytosolic chaperones, Hsp70 and Hsp90, are themselves controlled by regulatory ‘co-chaperone’ proteins. My research investigates the biochemical mechanisms of these regulated chaperone systems, how they function in protein folding and in the biogenesis of organelles such as mitochondria.