Positions

Structural biology of extracellular matrix proteins-- combining X-ray crystallography, cross-linking/mass spectrometry, and electron microscopy [Read more] about Deborah Fass

Laminin is a major component of the extracellular matrix (ECM) and arose early in animal evolution. Due to its role in cell adhesion and migration, laminin is central to development and disease. Laminin is a heterotrimer with a total mass of up to 800 kD. Its three subunits (α, β, and γ) assemble into a distinctive cross-shaped structure, copies of which further self-assemble to form a network. Higher organisms contain a number of isotypes of each subunit, which produce, combinatorially, a rich family of related proteins with certain structural and functional distinctions. Many fundamental aspects of laminin structure are understood from rotary shadowing electron microscopy, recognizable amino acid sequence motifs (i.e., coiled-coil heptad repeats), and X-ray crystallography of laminin fragments. However, other conserved portions of laminin, namely the L4, LF, and Lβ knob domains, are still poorly understood, both structurally and functionally. The L4 and LF domains are embedded within the EGF-like repeats that make up the short arms of the laminin cross, whereas the Lβ knob is inserted into the coiled-coil that constitutes the long arm of the cross. Until we determine the structures and functions of these embedded domains, our understanding of laminin and its binding and signaling capabilities will remain incomplete. This research project offers a rotation student the opportunity to work with Ph.D. students in the lab to learn protein purification and X-ray crystallography, as applied to the structures of key segments of laminin. The rotation student would also have the opportunity to be introduced to novel techniques in electron microscopy. Overall, the lab aims to combine a variety of structural and cell biological approaches to advance our understanding of laminin and its relation to other ECM components and to cells.

mechanism of an enzyme that catalyzes disulfide bond formation extracellularly to build the cell microenvironment

Rapid response against Zika Virus [Read more] about Ron Diskin

Join our recently initiated effort to combat Zika Virus

Structural and mechanistic characterization of the human protein disaggregation network

NMR studies of transient chaperone-substrate interactions

NMR studies of HIV-1 envelope glycoprotein and its interactions. [Read more] about Jacob Anglister

The work involves expression and purification of the HIV-1 envelope glycoprotein from a cell-line expressing the protein. Preparation of NMR samples. Learning the principles of NMR studies of proteins. Measurements of NMR spectra and their analysis.

Biomineralization or antibodies against structured surfaces

A combined biomedical/structural research aimed at understanding the mode of transfer of 4 phospho panthoteneic acid (P-Pant) from CoA onto acyl carrier protein and domains (ACP), key protein complexes in Mycobacterium tuberculosis causing the disease. [Read more] about Zippora Shakked

To find a better cure for tuberculosis we conduct a combined biomedical/structural research aimed at understanding the mode of transfer of 4 phospho panthoteneic acid (P-Pant) from CoA onto acyl carrier protein and domains (ACP), key protein complexes in Mycobacterium tuberculosis causing the disease. We look for M.Sc. students with a possible continuation towards a Ph.D. degree. The work will be conducted in the department of Structural biology, Weizmann Institute, as a collaboration between Prof. Zippi Shakked and Dr. Oren Zimhony from the Infectious disease unit, Kaplan Medical Center affiliated to the Hebrew University and Hadassah. For details please contact: Prof. Zippi Shakked : email: zippi.shakked@weizmann.ac.il and Dr. Oren Zimhony: email: oren_z@clalit.org.il and/or oren_zimhony@hotmail.com

Getting hands-on structural and diverse microscopic methods for studying cellular and viral processes.


Discover new principles of protein organization in cells using a mixture of computational and experimental approaches. Keywords: protein structure, protein evolution, protein interactions, yeast genetics, structural systems biology [Read more] about Emmanuel Levy

In a single yeast cell, the protein machinery is made of an estimated 50,000,000 protein molecules. Understanding how these proteins are organized in space and time with respect to each other to bring about life is a tremendous challenge central to biology, and at the core of our research. In order to understand principles of protein organization inside cells, we use both in vivo and in silico approaches. These involve biochemistry, protein engineering, genetics, high-throughput screens, as well as in silico analyses of biological data - in particular of structural and network data.

You can check the web-site for more information: www.elevylab.org

Combating deadly viruses [Read more] about Ron Diskin

Arenavirueses are a group of viruses that can cause severe human disease with high mortality rates. We study the recognition of cellular receptors by arenaviruses to understand the biology of the cell entry process and to develop future therapy. During a rotation project you will utilize molecular and structural biology techniques, tissue culture, protein expression and purification via chromatography and other general lab techniques, providing you with a comprehensive overview of our research. Please contact me for additional details.

Synthetic biology: Design of a protein chaperone [Read more] about Emmanuel Levy

The classic quote from Richard Feynman "What I cannot create I do not understand" best summarizes the motivation for this project, which goal is to design a chaperone based on a protein that is not itself a chaperone. This should reveal what properties are key to chaperones and thereby provide a proof that we understand how chaperones function.

We study the DNA-binding dynamics of transcription factors using single-molecule fluorescence spectroscopy. In your rotation, you will express, purify, and fluorescently label proteins and DNA.

Single-molecule dynamics in stochastic phenotype switching. [Read more] about Hagen Hofmann

You will recombinantly express and purify the transcription factor ComK, which is responsible for a stochastic phenotype switch in bacteria. After labeling DNA with fluorophores, you will use single-molecule FRET experiments to investigate the affinity of ComK for its promoter sequence.

Single-molecule fluorescence spectroscopy of protein interaction and dynamics

Single-molecule fluorescence spectroscopy of protein interactions and dynamics