X-Ray Crystallography of Chicken Egg-White Lysozyme
- Leila Bentaous
- Mariah Dicksen
- Drew Doubleday
- Krystian Glowac
- Sierra Goldstein
- Michelle Hajduk
- William Kane
- Norma Duke (Argonne National Laboratory, SER-CAT)
Proteins have three levels of structure with an optional fourth: primary, secondary, tertiary, and quaternary. The primary structure is the polypeptide chain of amino acids. The secondary structure is the beginning of the 3D shape of the protein. This structure uses Hydrogen Bonds to form either an α-helix or 𝛽-pleated sheet. The tertiary structure is what is focused on in this experiment. The protein becomes functional in the tertiary stage. This stage involves several types of bonds between the R-groups to form a folded, three dimensional structure of the protein.
Protein crystallography takes the pure protein solution and creates a form that allows for accurate data. When the protein is still in liquid form, the x-rays will scatter off in very random directions and it will be impossible to receive any information of the shape of that protein. The crystallized form aligns the proteins in the same orientation. The x-rays will scatter from the protein crystal and allow data to be gathered about the shape and structure of the protein.
This research is focusing on solving the protein structure of chicken egg-white lysozymes. Crystals will be grown, frozen in liquid nitrogen, mounted at the beamline, and diffraction data will be collected. Collected data will be analyzed in order to solve the structure.