Most, if not all, of my conclusions are wrong. However, if you disagree, you must explain why my conclusion is not consistent with the observations of the database, or provide an alternative conclusion that is consistent with the observations made about the mutant hemoglobin database, and that shows why my conclusion is probably wrong. Most mutant hemoglobins in the database are single amino acid substitutions. Most of the mutant hemoglobins in the database have a different net charge than that of normal hemoglobin Hemoglobin mutations in the database were not evenly distributed, being rarely observed at residues in the active site or at other amino acid residues that are obviously important for oxygen binding. Since most of the mutant hemoglobins in the database are very similar to normal hemoglobin in their overall properties, a single amino acid substitution has little affect on protein structure and activity.
Most spontaneous mutations change the net charge of hemoglobin.
When determining the kinetic properties of an enzyme, is it generally better to allow the reaction rate to stabilize rather than measuring the reaction rate immediately after combining the enzyme and substrate.