Research Spotlight:
Professor Mario bianchet
Meet ProfessoR Mario Bianchet
Mario Bianchet is an Associate Professor of Neurology, Biophysics & Biophysical Chemistry at Johns Hopkins School of Medicine. He received his Ph.D. in Physics from the Universidad Nacional de La Plata. His work focuses on macromolecules and the relationship between their structure and their biological function and dysfunction, particularly on human diseases.
Q: What is the focus of your research?
MB: “I conduct research on macromolecules that are relevant to the biomedical field. My focus is on understanding the relationship between their biological function and dysfunction and their three-dimensional structure, with a particular emphasis on diseases. To do this, I use various methods such as Biochemical, Molecular Biology, and Biophysical techniques like diffraction and small-angle scattering of X-rays, cryo-electron microscopy, computer modeling, and molecular dynamics simulation. My research has yielded 75 publications in high-impact journals with 4635 citations, an h-index of 38, and more than 70 structural entries in the protein databank (PDB).”
Q.Your research utilizes computer modeling and simulations to understand the relation between the structure of macromolecules and their biological function involved in human diseases. What is the process of creating these simulations?
MB: “Proteins and enzymes undergo various states to perform their essential biological functions. These functions encompass producing crucial compounds, applying forces, detecting signals, initiating channels to eliminate waste, and accumulating nutrients. However, structural methods like X-ray crystallography and Cryo-electron microscopy can merely capture a restricted number of snapshots of these states, limiting their efficacy in understanding the complete picture of these intricate processes.”
Q. What is the impact of computer modeling and simulations on your research?
MB: “Through computer modeling and simulation, we can enhance the results obtained from structural methods. This technique allows us to explore the different states of a macromolecule during its functioning. We can use Molecular Dynamics to simulate the protein’s temporal evolution in the cell environment to determine transport pathways, identify crucial residues that may cause genetic diseases when mutated, and more.”
Q: Your current research interest includes neurodegenerative diseases associated with viral infections. How has computing impacted the way we research and understand these neurodegenerative diseases?
MB: “One of the research analyses done in ARCH allowed to study the stability of a proposed model of neurotoxic fibril of HIV-Tat protein. The report is in preparation.”
Q. What inspired you to pursue a research career in structural biology?
MB: “Curiosity of how protein and enzyme (these submicroscopic machines) use the laws of the physics to make functioning organisms.”
Q.What is the impact or value of Rockfish on your research?
MB: “The prestigious journal Nature recently published a report on the structure of Na+/I- symporter (NIS), which presented the results of Cryo-electron microscopy and molecular simulations performed on ARCH.”
Ravera S., Nicola J.P., Salazar-De Simone G., Sigworth F.J., Karakas E., Amzel L.M., Bianchet M.A., Carrasco N. Structural insights into the mechanism of the sodium/iodide symporter (2022) Nature, 612 (7941), pp. 795 – 801.