NSF REU at K-State: Interactions of Matter, Light and Learning

The K-State REU program offers summer fellowships to do world-class research in our friendly physics department in the scenic Flinthills. We are funded by the National Science Foundation.

Soft Condensed Matter and Biophysics

Modeling Pathway Selection in Biomolecule Aggregates (Theory)

Jeremy Schmit

Email: schmit@phys.ksu.edu

The way that biomolecules assemble into higher order structures can make the difference between properly functioning nano-machines or aggregates that cause diseases. One type of pathological assembly is an amyloid fibril, which appears in many diseases including Alzheimer's, Huntington's, Parkinson's, and type II diabetes. The fact that similar protein aggregates are found in all these diseases suggests that a treatment targeting the aggregation pathway could alleviate many of these disorders. This project will attempt to identify the aggregation pathway by examining the physics by which proteins discriminate between ordered and disordered assembly pathways. It will involve developing computer code (Mathematica, C++, Python, or other) to simulate the binding lifetimes as incoming molecules attempt to join an existing aggregate. These simulations will be compared to existing experimental data to determine how pathological aggregates form.

How do Phase Separated "Factories" Assemble Molecular Machines (Theory)

Jeremy Schmit

Email: schmit@phys.ksu.edu

In recent years the biophysics community has been buzzing with the discovery that many cellular structures are formed by phase transitions. One such structure is the nucleolus, which serves as a molecular factory to assemble ribosomes. However, unlike man-made factories, which have carefully arranged machines and conveyor belts, the nucleolus is a disordered liquid. The goal of this project is to determine how interactions within the liquid facilitate the assembly of complex molecular machines. This will be done using simple computer simulations to model how ribosomal components bind and release from their surrounding molecules as they search for the unique assembly that allows them to perform their function.