Office: Bioinformatics 231
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Our research area is experimental biophysics. We are trying to understand the molecular logic underlying biological function. By nature, the research is highly interdisciplinary. Students will learn spectroscopic techniques (Nuclear Magnetic Resonance (NMR), circular dichroism (CD), fluorescence), molecular modeling, and gain basic biochemistry skills.
DNA transposition is the mechanism that can be used to deliver genetic information to mammalian genome. It has been employed for gene therapy and for functional genomics studies. The Sleeping Beauty (SB) transposon system is the most frequently used DNA transposon in functional genomics, and is the first and only DNA transposon that has been adapted for human gene therapy. The SB system consists of the transposase enzyme and of the transposon DNA. From the biophysics point of view, the SB transposition is the sequence of steps during which the transposase interacts with the transposon DNA. Accordingly, we study these steps to create a dynamic picture with atomic-level resolution of how molecular components of the SB transposon system work together.
Chemokines form a large family of proteins that guide the migration of leukocytes in our body. We need chemokines to fight the infection, but they can also play a negative role by promoting autoimmune and allergic inflammatory reactions, cancer, atherosclerosis, or other inflammatory disorders. Chemokines act individually or interact to form heterooligomers. These interactions alter the biological activity of individual chemokines. We are looking at different chemokines to describe their interactions at atomic level in order to design molecule that will block (or enhance) the interactions, because we believe that it may lead to the development of more targeted, anti-inflammatory pharmacological agents with minimal side effects.
Biological processes depend on diffusive transport of molecules within cell and tissue. The first step of a biochemical reaction is the translational diffusion of at least one species to recognize another species involved in the reaction. To date, the translational diffusion of biopolymers, primarily globular proteins, has been studied in dilute solutions – idealized conditions required in most biophysical studies. We aim to understand the diffusion of biopolymers in solution in a wide range of concentrations when crowding is created by like or dislike molecules.
The key challenge here is to be able to synthesize protein-stabilized Au NCs in a predictable and controllable manner using the whole variety of functionally important proteins. Thus far, only standard proteins such as lysozyme, bovine serum albumin (BSA), insulin, trypsin, and a few other proteins have been used to synthesize Au NCs. These studies provide the proof of principle and suggest that protein Au NC complexes can be formed by many proteins. However, the understanding of (i) protein-NC formation process, (ii) protein-NC interactions, and (iii) overall protein-NC conformation and stoichiometry, is still lacking. Since the protein plays a vital role in stabilizing, reducing, and arranging gold atoms into stable nanoclusters, the formation of a single Au NC product would be highly dependent on the conformation of the protein. Thus, a comprehensive characterization of protein-stabilized Au NCs is in high demand, and we intend to fill this gap.