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Department of Structural Biology
Amnon Horovitz, Head
Structural biology is an increasingly important and exciting area. At the Weizmann Institute, much of the research in this area is carried out in the Faculty of Chemistry. Current research projects involve utilization of the main methodologies available for biological structural studies, such as X-ray crystallography, NMR, electron microscopy, molecular biology and various other spectroscopic techniques. Modern and sophisticated instrumentational facilities are available, most of which are state-of-the-art. Studies are being performed to determine molecular structures and structure-function relationships in biological macromolecules, such as proteins, DNA chains and their complexes. Efforts are directed towards the design of potential drugs. Whole intracellular assemblies and organelles, such as the ribosomes, which contain tens of macromolecules, are being investigated. The powerful techniques of site-directed mutagenesis and thermodynamics are being used to characterize, in detail, the interactions that stabilize proteins and determine their activity. Antigen-antibody complexes and other protein-protein interactions such as that of interferon with its receptor are being studied by multi-dimensional NMR methods. Biomineralization, i.e. controlled mineral deposition by organisms to form skeletal tissues, is being investigated from the molecular interactions between proteins and crystals to the ultrastructure and properties of the tissue.
L. Addadi
lia.addadi@weizmann.ac.ilMechanisms of crystal nucleation and modulation of crystal growth and properties in biomineralization (bone, mollusk shells, echinoderms).
L. Addadi, S. WeinerAntibodies that recognize crystal surfaces and 2-dimensional organized patterns.
Mechanism of cell adhesion using crystal substrates.
L. Addadi, B. Geiger
J. Anglister
jacob.anglister@weizmann.ac.ilThe structure of the V3 loop ohf HIV-1 enevelope protein gp120
J. Anglister, S. Zolla-PaznerNMR structure of alpha Interferon complex with its receptor
J. Anglister, G. SchreiberNMR structure of the alpha subunit of the acetylcholine receptor
J. Anglister, ZZ. WangThe structure of the transmembrane glycoprotein of HIV-1 gp41.
J. Anglister, Y. Shai
D. Fass
deborah.fass@weizmann.ac.ilStructures of retrovirus envelope proteins and mechanisms of retrovirus entry into cells.
Structure and function of proteins that modulate intracellular membrane dynamics.
Origins of disulfide bonds for oxidative protein folding.
A. Horovitz
amnon.horovitz@weizmann.ac.ilAllostery in the structure and function of GroEL and CCT chaperonins.
LFER analysis of allosteric transitions in proteins.
Chaperonin-mediated protein folding.
K. Muszkat
alex.muszkat@weizmann.ac.ilCIDNP and NMR studies of proteins: conformations, protein-protein interactions, binding, and protein folding under physiological conditions.
CIDNP and NMR studies of antigenic and immunogenic peptides and their conformations. CIDNP studies of transient conformations of proteins and peptides.
Synthesis of cyclic peptides incorporating Y-E epitopes.
M. Safro
mark.safro@weizmann.ac.ilCrystal structure of cytoskeletal proteins: vinculin, E-cadherin.
M. Safro, B. GeigerHuman phenylalanyl-tRNA synthetase: cloning, expression, 3-D-structure, drug-design.
X-ray analysis of phenylalanyl-tRNA synthetase from Th. Thermophilus and its complexes with functional ligands: tRNA, PheAMP, etc.
I. Sagi
irit.sagi@weizmann.ac.ilStructural -Dynamic studies of Metalloenzymes and Protein-Nucleic Acid Interactions.
Our research covers a wide range of areas with the common themes of dynamic structure-function investigations. The principle areas of investigation are mechanism of action of metalloenzymes and protein-nucleic acid interactions. Our objective is to study
Z. Shakked
zippi.shakked@weizmann.ac.ilCrystal structure and solution studies of DNA oligomers.
Z. Shakked, Donald Crothers (Yale University)
- DNA regulatory elements
- DNA bending by adenine-thymine tracts
Structural and biochemical studies of proteins involved in transcriptional regulation.
- The tumor-suppressor protein p53 and its interaction with DNA and the basal transcription machinery
- The leukemia-related RUNX1(AML1) transcription regulator
J. Sussman
joel.sussman@weizmann.ac.ilX-ray structural analysis and molecular biology studies on proteins from the nervous system, including acetylcholinesterase (AChE), human, torpedo, drosophila, and krait; butyrylcholinesterase; neural cell adhesion proteins with sequence similarity to ACh
Structure based drug design studies on AChE and beta-secretase, including studies of complexes with transition state analogs; potential drugs for the treatment of Alzheimer's disease; and snake neurotoxins.
3D structural studies of halotolerant proteins from unicellular alga Dunaliella.
Application of ultra rapid X-ray diffraction methods to study the enzymatic mechanism of AChE in real time.
3-D structure analysis and prediction of protein structures; and design and construction of a large object oriented relational data base for 3D structures of biological macromolecules found in the protein data bank.
S. Weiner
steve.weiner@weizmann.ac.ilArchaeological science: minerals and molecules in the sediments of the archaeological record.
Structure - mechanical function relations in mineralized tissues (bone and teeth).
S. Weiner, H.D. WagnerBiomineralization: mechanisms of mineral formation and growth in biology.
S. Weiner, L. Sddadi
A. Yonath
ada.yonath@weizmann.ac.ilRibosomes: structure analysis by X-ray crystallography.
Antibiotics of protein biosynthesis.
Molecular Genetics and biochemistry of ribosomal RNA and proteins.
This file was last modified on 03/06/2012 13:42:09
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