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The Alexander Silberman Institute of Life Science
Eitan Lerner
Dr. Eitan Lerner
Single-Molecule Biology
Biological Chemistry
Personal Information
Research Interests
- Pre-genetic mechanisms promoting development of bacterial resistance to antibiotics
- Characterization of oligomers of the alpha-Synuclein protein as factors in the development of Parkinson's disease
- Allosteric signal transmission through DNA
- Method development for structural characterization of proteins in Vivo
Dissertation Topics
- Determination of the structure of the bacterial transcription complex in states that evade antibiotic inhibition, using single-molecule spectroscopy and computational models.
- Method development for determination of protein structures inside the cell, using single-molecule spectroscopy and computational models.
- Characterization of the α-Synuclein oligomers: The protein α-Synuclein (α-Syn) is a central player in the development of Parkinson's disease (PD). This protein tends to bind to its partner α-Syn proteins, and by that to form fibrils that do not dissolve in the cellular medium. The nucleation process of such a fibril involves many α-Syn oligomers, with many different sizes and structures. Most probably, most of these oligomers do not contribute to the formation of the fibril. On the other hand, it is known that there is a subset of these oligomers that tend to adsorb onto cellular membranes. The project aim: characterizing the oligomers of α-Syn that adsorb to cellular membranes, and by that act as cell toxicity factors in the development of PD. The characterization will be performed using a combination of single-molecule spectroscopy measurements and computational modelling.
- The study of allosteric signal transmission mechanisms in biology in general and through DNA in particular: in allostery ligand 1 that binds a protein at a binding site A, modulates that affinity of ligand 2 to a binding site B on that protein, distant to binding site A. And so, mechanical communication is enabled through the protein. What is the mechanism by which allosteric signal transmission is enabled? Is it possible to design proteins and DNA with engineered allosteric characteristics? Can DNA-binding proteoins (DBPs) "report" their position on DNA to other distant DNA-bound DBPs by allosteric signal transmission over DNA?
