deletions | additions       diff --git a/Results_Protein_production_and_baseline__.md b/Results_Protein_production_and_baseline__.md  index afeedf3..80d0f6c 100644  --- a/Results_Protein_production_and_baseline__.md  +++ b/Results_Protein_production_and_baseline__.md 
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# Results   ## Protein production and baseline values   In total, 117 proteins, including native BglB, were purified with immobilized metal affinity chromatography and eluted in 200 μL HEPES buffer. Of the 117 proteins synthesized, 79 proteins express and purify as soluble protein. Greater than 65% of mutants maintained the yields obtained by native BglB while roughly 30% did not express and purify as a soluble protein above our limit of detection (0.1 mg/mL) for protein yield after purification based on A280 and SDS-PAGE. Of the 85 79  proteins with expression, 69 mutants displayed a melting temperature that fit to our logistic equation. Native BglB displayed an average melting temperature of 39.6 C. [Summarize protein production specifics]  ## Thermal stability of mutants compared to wild type   Acrossall  69 point mutations, the average melting temperature was 38.9 degrees C (plus or minus __ C) __C)  while the average kurtosis was -0.7501861. __% 58%  of mutations were within one degree of the native BglB. The BglB, indicating the  overall effect of point mutations was minimal onmelting temperature, suggesting single point mutations do not illicit a strong affect on  protein structure. The melting temperature range of all point mutations was 33.8 degrees C to 45.3 degrees C, a deviation of roughly six degrees in either direction from that of native BglB. __% and __% C. 36%  of mutations displayed a  higher melting temperatureand lower melting temperature, respectively,  than that of native BglB. [Describe what we found regarding the range of thermal stabilities we observed]