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AS Human Biology Unit 4


Text questions

P57/Q1   Condensation.
 
P62/Q2   37 C is the optimum temperature for enzymatic activity.
 
P62/Q3   Protein has denatured.
 
P65/Q4   pH is the stomach is low → amylase will denature in the stomach.
 
P67/Q5  
Competitive inhibitor (CI) Non-competitive inhibitor (N-CI)
CI's molecule is similar to that of the enzyme's true substrate → it fits into the active site and forms an enzyme-inhibitor complex → true substrate is not able to enter the active site. N-CI's molecule is not similar to the molecule of the substrate. However N-CI can fit in a "pocket" on the enzyme (other than the active site). As a result the globular structure of the enzyme is altered and so is the shape of the active site → the true substrate is not able to enter the active site.


Assignment

P70/Q1 a) The external surface of the ripe tomato will bulge in more.
 
  b) Your ideas here...
 
P71/Q2 a) Juice extractor ?
 
  b) Measure the time needed for 100ml of the Certo solution to flow down through a narrow funnel (into a beaker) ?
 
  c) Your ideas here...
 
P71/Q3   Your ideas here…
 
P71/Q4   Temperature, pH, concentration of enzyme and substrate, presence of inhibitors
 
P71/Q5   Your ideas here…
 


Examinations

P72/Q1 a) Activation energy = energy needed to bring molecules together so that they will react with each other.
 
  b) (i) The Lock & Key hypothesis. An enzyme described as a rigid structure. The enzyme active site is a negative impression of the molecule of the substrate. Substrate arrives at the active site of the enzyme → thanks to intermolecular forces of attraction/hydrogen bonds, the molecule of the substrate fits into the active site → the molecules are rearranged there to form products → products leave active site.

(ii) The Induced Fit hypothesis: an enzyme is described as a flexible, elastic, "wobbly" structure. Substrate arrives at the active site. Thanks to some intermolecular forces of attraction/hydrogen bonds, the molecule of the substrate fits into the active site of the enzyme. The active site of the enzyme is not a negative impression of the molecule of the substrate → the shape of the molecule of the enzyme is altered by a slightly different shape of the molecule of the substrate. The distorted molecule of the enzyme in turn distorts the substrate in the resulting enzyme-substrate complex. Strains/tensions created within the molecule of the substrate lower the activation energy needed for the chemical change (reaction) to occur.
 

  c) 2H2O2 → 2H2O + O2 (gas) by catalase

As O2 (gas) evolves and escapes to the atmosphere, the mass of the contents of the beaker drops.
 

  d) The concentration of the enzyme remained the same, yet the concentration of the substrate dropped → lower ratio of substrate molecules: enzyme molecules → fewer collisions → lower rate of reaction.
 
P72/Q2 a) A molecule of the competitive inhibitor (CI) has a similar shape to the molecule of the true substrate → CI takes the substrate's place at the enzyme's active site → fewer active sites available for the molecules of the true substrate → lower enzyme concentration → lower rate of reaction.
 
  b) The limiting factor is the concentration of the enzyme. Until its concentration is higher, the rate of reaction will not increase because the turnover rate of an enzyme is a fixed value.
 
  c) The ratio "substrate : enzyme" will increase, while the ratio "CI : enzyme" will stay the same. Hence more collisions between enzyme and substrate → higher rate of reaction.
 
 

 

 

 

 

 

 
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