Chemistry, 19.02.2020 04:01 Juicebox18
A useful method to assay many hydrolytic enzymes is to follow enzymatic activity by determining production or uptake of hydrogen ions during the reaction. For example, consider a protease that catalyzes cleavage of internal peptide binds in a protein:
Assume the enzyme is fully active at pH 8.8, that the pKa of an a-carboxyl group in a peptide is 3.5, and that the pKa of an a-amino group in a peptide is 8.5. How will the action of this protease on a protein affect the pH of an unbuffered reaction mixture (starting at pH 8.8)? Explain your answer.
The protease reaction is run in a pH-stat, a device that maintains a constant pH in a reaction mixture by continuous, automatic addition of acid or base. The instrument has a recorder that plots the volume of acid or base added versus time of the reaction. If the action in (a) is run in a pH-stat maintained at pH 8.8, calculate the millimoles of titrant that must be added per millimole equivalent of the peptide bonds hydrolyzed by the enzyme.
Answers: 2
Chemistry, 22.06.2019 03:40
Kc = 0.040 for the system below at 450oc. if a reaction is initiated with 0.40 mole of cl2 and 0.40 mole of pcl3 in a 2.0 liter container, what is the equilibrium concentration of cl2 in the same system? pcl5(g) ⇄ pcl3(g) + cl2(g)
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Chemistry, 23.06.2019 01:30
Ascientist conducted an experiment and discovered that certain plants grow faster when given a particular amount of fertilizer. anouther scientist conducted the same experiment and got similar results. which concept does this best illustrate? a) repetition b) replication c) precision d) validity
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A useful method to assay many hydrolytic enzymes is to follow enzymatic activity by determining prod...
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