Research

Protein engineers have successfully designed many proteins to either increase their thermostability or modulate their function, but less thought has been given to the interplay between these two goals. Our lab uses a pair of proteins to determine the balance between function in a native, DNA-binding protein and stability in its engineered, thermostable counterpart. We use biochemical assays to measure stability and function, and we perform molecular dynamics simulations to investigate the atomic-level interactions that drive stability and function. Our investigations will illuminate how to design new functions in proteins without compromising thermostability.

Once a simulation of protein dynamics is performed, the resulting trajectory consisting of the protein atoms’ coordinates over time is processed to draw quantitative conclusions about the protein’s motions. Our lab develops analysis tools in the ilmm software suite in order to better quantify protein motion in a general, high-throughput manner.