Faculty Sponsor's Department:
The 3D structure of a protein is integrally important to its function, so knowledge of the 3D structure is crucial to understand a protein’s function. Current techniques for determining protein structure include X-Ray crystallography, NMR spectroscopy and cryo-electron microscopy, but these all have limitations. Recent developments have shown that atom probe tomography can be used to characterize protein structure without requiring protein crystallization. To use this technique, individual proteins must be encapsulated in a solid. This project aims to embed proteins in silica glass beads in the proper configuration for use with atom probe tomography. A silica glass bead is formed by placing a droplet of a mixture of sodium silicate and protein solution in an acoustic ultrasonic levitator. The acoustic levitator allows the droplet to dry in an isotropic manner as water evaporates from its surface and a solid glass is formed. In this process, pH and composition of the mixture, drying time and droplet volume are manipulated. Protein distribution within the bead can be evaluated using UV-vis and fluorescence microscopy. In order to be analyzed, the glass bead can be fixed in an epoxy resin and sanded to expose a cross section of the bead. The goal of this project is to develop a procedure for synthesizing a silica glass bead with an ideal protein distribution for atom probe tomography.