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## Mutants have [effect] on thermal stability   A novel finding was a nearly six degree increase in melting temperature by single point mutant N404C. The BglB crystal structure reveals a weak hydrogen bond between N404 and the backbone of a L402. Molecular modeling of N404C predicts the loss of this hydrogen bond to the protein's alpha helix, in which the protein is allowed to repack into more energetically favorable states. Similarly, the removal of a weak hydrogen bond in point mutation W120F results in a marked increase in melting temperature, 42.5 C. The BglB crystal structure indicates a weak hydrogen bond between W120 and the backbone of N163. The mutation to the aromatic phenylalanine maintains the structural integrity at the mutation site as well as removes the hydrogen bond to the neighboring alpha helix. The increased stability is probably attributed to improved packing in the protein's structure upon the removal of the hydrogen bond whilst preserving the general size and aromaticity at the mutation site. Previous studies have shown a similar increase in stability upon tryptophan to phenylalanine point mutations \cite{Fulton_2003}  . Conversely, a greater than five degree decrease in melting temperature was observed in single point mutation H178A. The BglB crystal structure displays a strong hydrogen bond between H178 and a neighboring alpha helix. Molecular modeling displays H178A loses this essential interaction in the protein structure, resulting in its readily unfolding at higher temperatures. Likewise, point mutation E222H had a melting temperature of 34.7 C, a nearly five degree decrease than that of native BglB. Previous studies show strong hydrogen bond interaction, 2.6 and 3.1 Å, between E222 and its neighboring R240 residue \cite{Carlin_2016}. The introduction of histidine at the mutation site causes the loss of these strong hydrogen bonds as well as the creation of electrostatic repulsion between the partially positively charged and positively charged amino acids. The cumulative effect of this mutation results in the protein's decreased stability at lower temperatures.