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[Summarize protein production specifics]  ## Thermal stability of mutants compared to wild type   The melting temperature determined for wild type was 39.6 C. The average melting temperature across all point mutations was 40.7 degrees C (plus or minus .7 C). The overall effect of point mutations was minimal on melting temperature, suggesting that point mutations generally do not affect the protein structure. However, at certain residues, these point mutations have a large effect on the stability of the protein. The melting temperature range for the mutants was 33.8 degrees C to 45.3 degrees C, a deviation of six degrees in either direction from that of wild type. Mutation N404C increased the protein's stability as it displayed a melting temperature of 45.3 C. Conversely, mutation H178A displayed a substantial decrease in protein stability with a melting temperature of 33.8 degrees C. [Describe what we found regarding the range of thermal stabilities we observed] ## Mutants have [effect] on thermal stability   Certain mutations that significantly alter the protein's structural integrity result in a less thermostable enzyme. The mutation E222H displayed a lower melting temperature than that of wild type's by nearly 5 degrees. A neighboring R240 residue has two hydrogen bonds to the E222 residue, creating strong interactions which stabilize the protein's structure. Mutating this residue to histidine removes these strong hydrogen bonds and creates electrostatic repulsion with the neighboring arginine, compromising the protein's structure.   [Describe what we found here]