Group Final Project

Group: Alya, Beyza, Sydney, Zander.

Brainstorming session

Bacteriophages -> L to lyse bacterial cells Release newly produced phages Modification to make more effective for lysing the protein Higher stability for L protein L protein interacts with host (cellular missionary) with chaperone, DnaJ Influence protein folding POSSIBLE DIRECTION: modifying residues to influence how L protein interacts with host proteins Specific minor acid residues can affect lysis

GOALS Increase stability of L protein Higher titers Higher toxicity of lysis protein

COMPUTATIONAL DIRECTIONS Attempt to improve L stability Computational protein design tools Investigate mutations that could impact protein and host factors interactions

Pull from database what is considered more stable from similar proteins See what is conserved between them What does stability mean in this context? Only in cytosol? Ultimate method of delivery? Use same tool for Week 5 Host cell in unfolded, folded by chaperone POSSIBLE DIRECTION: If the efficacy of L protein requires chaperone (working within specific temp range), could we mutate to work in greater temperature range for that chaperone Limit denaturation? Binding (30-37 C) -> will not be able to lyse bacteria

READING (BEFORE NEXT MEETING) Stability, which parts of protein to stability Binding characteristics What we can change, play with