As a postdoctoral research scientist
HSF1 or heat shock factor 1, is an important transcription factor protein present in all cells. This factor can bind to target DNA sequences that encode specific proteins called molecular chaperones. This function is vital when cells experience stress such as changes in temperature, chemical imbalances, etc. and is responsible for increasing the production of molecular chaperones under such conditions. This increase in molecular chaperones helps to prevent the ultimate death of a cell as a result of the mass accumulation and aggregation of proteins in the cell.
Although this protein, due to its importance, has been studied extensively for over 30 years by researchers all over the world, there was a fundamental question that still needed to be answered; What does the protein structure look like? I was curious to find out the answer to this question when I joined the Dept. of Cellular Biochemistry and the lab of Dr. Ulrich Hartl at the Max Planck Institute for Biochemistry in Munich. It was a risky project because people in the field have tried before, but as I have always thought to myself “no risk no glory!”
The publication related to our findings can be found here. In addition, I had a fruitful collaboration with an amazing crystallographer/biochemist in the lab, Dr. Andreas Bracher. I had the opportunity to write a book chapter and a mini-review with him. They can be accessed here.