30 Questions
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
What is the purpose of using a basic condition in the Sanger Reagent method?
To facilitate the displacement of the F-(NO2)2Phenyl group
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
What is the role of the organic solvent in the Sanger Reagent method?
To extract the derivative of the first amino acid
What is the purpose of repeating the Edman Degradation reaction?
To determine the sequence of the polypeptide
What is the product of the reaction between the Sanger Reagent and the polypeptide under acid conditions?
Phenyl-NH-Ala-COOH + NH3-Gly-COOH + NH-Phe-COOH
What is the primary benefit of the induced-fit model of enzyme action over the lock-and-key model?
It allows for a greater range of substrate specificity
What is the role of the active site in the lock-and-key model of enzyme action?
It has a rigid shape that only fits specific substrates
What is the equation that represents the overall reaction of enzyme-catalyzed reactions?
E + S → ES → E + P
Why do enzymes increase reaction rates?
They decrease the activation energy
What happens when a substrate fits properly in an active site?
An enzyme-substrate complex is formed
What is the region on the enzyme molecule where the substrate binds?
Active site
What is the advantage of the enzyme-substrate complex formation in terms of catalysis?
It improves the fit between the enzyme and substrate, increasing catalysis
What is the term for the enzyme without its non-protein moiety?
Apoenzyme
What is the type of cofactor that is tightly bound to the apoenzyme by covalent bonds?
Prosthetic group
What is the complex formed when a substrate binds to an enzyme?
Enzyme-substrate complex
What is the term for the active enzyme with its non-protein component?
Holoenzyme
What is the type of cofactor that is loosely bound to the apoenzyme by non-covalent bonds?
Coenzyme
What is the primary reason why extreme temperatures can be detrimental to enzymatic activity?
They denature the enzyme, causing it to unfold
What is the term for the temperature at which an enzymatic reaction occurs at its fastest rate?
Optimum temperature
What is the role of cofactors and coenzymes in enzymatic activity?
They are inorganic substances and vitamins that facilitate enzymatic activity
What happens to the rate of reaction when the substrate concentration increases, while the enzyme concentration remains constant?
The rate of reaction increases
What is the effect of a competitive inhibitor on the rate of an enzymatic reaction?
It decreases the rate of reaction
What is the term for the pH at which most enzymes have their maximum activity?
Neutral pH
What is the primary biochemical activity of Ligases?
Join two molecules with covalent bonds
Which type of enzyme is Phenylalanine hydroxylase?
Transferase
What is the primary biochemical activity of Isomerases?
Catalyse isomerization changes within a single molecule
Which type of enzyme is Fumarase?
Lyase
What is the primary biochemical activity of Phosphatases?
Catalyse the hydrolysis of various bonds
Which type of enzyme is Glutamine synthetase?
Ligase
Learn how to identify the amino acid present at the beginning of a sequence using chemical reactions and proteolytic enzymes. This quiz covers the Sanger method and its application in determining the sequence of amino acids in polypeptides.
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