Final answer:
The effect of mutations at positions 216 and 226 on trypsin cannot be definitively determined without the referenced Figure 1 and Table 2. Missense mutations can cause amino acid substitution, potentially affecting enzyme activity. Specific amino acids in the active site are essential for enzymatic catalysis.
Step-by-step explanation:
The question asks what effect the mutation of Gly-216 to threonine and Gly-226 to valine on Trypsin would have. The enzyme trypsin is known to preferentially cleave peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. Amino acid substitutions at positions 216 and 226 could alter the specificity or catalytic activity of trypsin, depending on the properties of the substituted amino acids compared to glycine. While the provided information does not directly answer the question, amino acid substitutions can critically affect enzyme activity; for instance, missense mutations can lead to amino acid substitution altering the enzyme's structure and function. Additionally, the active site of an enzyme is usually composed of a small percentage of the enzyme's structure where specific amino acids like His, Cys, Asp, Arg, and Glu play critical roles in catalysis. Based on this, we might infer that mutations in trypsin could either increase or decrease its specificity or catalytic activity. However, without additional specific data from 'Figure 1' and 'Table 2' the student is referring to, it is impossible to provide a definite answer. A guess would not be appropriate as it could mislead the student.