Y1S2 003 III Biochem Determining Amino Acid Sequence in Proteins
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Questions and Answers

What is the primary limitation of using the Sanger Reagent method to determine the sequence of a polypeptide?

  • It destroys the rest of the polypeptide chain (correct)
  • It is unable to label the first amino acid
  • It requires a large amount of the polypeptide
  • It is only applicable to simple polypeptide chains

    • What is the purpose of using a basic condition in the Sanger Reagent method?

  • To facilitate the displacement of the F-(NO2)2Phenyl group (correct)
  • To enhance the extraction of the derivative
  • To denature the polypeptide chain
  • To break the bonds at specific points

    • What is the primary advantage of using the Edman Degradation method over the Sanger Reagent method?

  • It does not destroy the rest of the polypeptide chain (correct)
  • It allows for the determination of the entire sequence of the polypeptide
  • It is faster and more efficient
  • It is less expensive and requires less reagent

    • What is the role of the organic solvent in the Sanger Reagent method?

    <p>To extract the derivative of the first amino acid</p> Signup and view all the answers

    What is the purpose of repeating the Edman Degradation reaction?

    <p>To determine the sequence of the polypeptide</p> Signup and view all the answers

    What is the product of the reaction between the Sanger Reagent and the polypeptide under acid conditions?

    <p>Phenyl-NH-Ala-COOH + NH3-Gly-COOH + NH-Phe-COOH</p> Signup and view all the answers

    What is the primary benefit of the induced-fit model of enzyme action over the lock-and-key model?

    <p>It allows for a greater range of substrate specificity</p> Signup and view all the answers

    What is the role of the active site in the lock-and-key model of enzyme action?

    <p>It has a rigid shape that only fits specific substrates</p> Signup and view all the answers

    What is the equation that represents the overall reaction of enzyme-catalyzed reactions?

    <p>E + S → ES → E + P</p> Signup and view all the answers

    Why do enzymes increase reaction rates?

    <p>They decrease the activation energy</p> Signup and view all the answers

    What happens when a substrate fits properly in an active site?

    <p>An enzyme-substrate complex is formed</p> Signup and view all the answers

    What is the region on the enzyme molecule where the substrate binds?

    <p>Active site</p> Signup and view all the answers

    What is the advantage of the enzyme-substrate complex formation in terms of catalysis?

    <p>It improves the fit between the enzyme and substrate, increasing catalysis</p> Signup and view all the answers

    What is the term for the enzyme without its non-protein moiety?

    <p>Apoenzyme</p> Signup and view all the answers

    What is the type of cofactor that is tightly bound to the apoenzyme by covalent bonds?

    <p>Prosthetic group</p> Signup and view all the answers

    What is the complex formed when a substrate binds to an enzyme?

    <p>Enzyme-substrate complex</p> Signup and view all the answers

    What is the term for the active enzyme with its non-protein component?

    <p>Holoenzyme</p> Signup and view all the answers

    What is the type of cofactor that is loosely bound to the apoenzyme by non-covalent bonds?

    <p>Coenzyme</p> Signup and view all the answers

    What is the primary reason why extreme temperatures can be detrimental to enzymatic activity?

    <p>They denature the enzyme, causing it to unfold</p> Signup and view all the answers

    What is the term for the temperature at which an enzymatic reaction occurs at its fastest rate?

    <p>Optimum temperature</p> Signup and view all the answers

    What is the role of cofactors and coenzymes in enzymatic activity?

    <p>They are inorganic substances and vitamins that facilitate enzymatic activity</p> Signup and view all the answers

    What happens to the rate of reaction when the substrate concentration increases, while the enzyme concentration remains constant?

    <p>The rate of reaction increases</p> Signup and view all the answers

    What is the effect of a competitive inhibitor on the rate of an enzymatic reaction?

    <p>It decreases the rate of reaction</p> Signup and view all the answers

    What is the term for the pH at which most enzymes have their maximum activity?

    <p>Neutral pH</p> Signup and view all the answers

    What is the primary biochemical activity of Ligases?

    <p>Join two molecules with covalent bonds</p> Signup and view all the answers

    Which type of enzyme is Phenylalanine hydroxylase?

    <p>Transferase</p> Signup and view all the answers

    What is the primary biochemical activity of Isomerases?

    <p>Catalyse isomerization changes within a single molecule</p> Signup and view all the answers

    Which type of enzyme is Fumarase?

    <p>Lyase</p> Signup and view all the answers

    What is the primary biochemical activity of Phosphatases?

    <p>Catalyse the hydrolysis of various bonds</p> Signup and view all the answers

    Which type of enzyme is Glutamine synthetase?

    <p>Ligase</p> Signup and view all the answers

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