I. s aso knowledge of the effects of pH on amino acid chains, R-group interactio
ID: 209043 • Letter: I
Question
I. s aso knowledge of the effects of pH on amino acid chains, R-group interactions and protein folding (specificall, consider secondary to quaterary protein structure of polypeptide chains),briefly answer the questions below Specifically, what do you hypothesize has happened to the active sites in the enzyme to explain the least maltose production? Above, the directions state that DNS stops the enzymatic reaction. What is one way that DNS could stop the enzymatic reaction that is different from the effect of pH on the enzyme? 2. You are a scientist working in a lab on a project to create starch from maltose. You have two tubes of identical, aqueous solutions, reactants, you regularly use in your work. You have labeled them with labelling tape and know that only one of them contains your enzyme and the other contains another solution. You were away from the lab for the weekend when the air conditioning failed in your lab and the labels have fallen off of your two identical aqueous tubes. You are unsure which is your enzyme of interest. Using the concepts of enzyme and the DNS methodology for visualization of the carbohydrate macromolecule, utilized today in lab, please write testable hypothesis to assign identity to the two tubes. Ho: HA:Explanation / Answer
Answer 1) Formulated Hypothesis; An Altered quaternary structure (shape) of amylase enzyme disrupts the active site for starch molecule binding under the non-optimal PH.
so, none of the starch molecules get converted into maltose.
DNS is a laboratory reagent which specifically reacts with the reducing molecules such as reducing sugar glucose (carbohydrate of starch) and makes it inevitable to react with amylase enzyme in DNS method.
it is different from PH because it affects the substrate and not the enzyme.