Treating a solution of ribonuclease with 2-mercaptoethanol and urea denatures the enzyme. If the 2-mercaptoethanol is removed, followed by the removal of urea, the ability of the enzyme solution to hydrolyse RNA is reduced by about 99%. What is the most plausible explanation for this observation?   a. All of the RNase molecules have about 1% of their usual activity, due to changes to the organisation of disulphide bonds   b. Random formation of disulphide bonds mean about 1% of the RNase molecules are 100% active whereas 99% have no activity   c. Deprotonation of histidine in the active site of the enzyme means that only about 1% of the enzyme molecules are active   d. Deprotonation of histidine in the active site of the enzyme means that all

Human Anatomy & Physiology (11th Edition)
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Chapter1: The Human Body: An Orientation
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Treating a solution of ribonuclease with 2-mercaptoethanol and urea denatures the enzyme. If the 2-mercaptoethanol is removed, followed by the removal of urea, the ability of the enzyme solution to hydrolyse RNA is reduced by about 99%. What is the most plausible explanation for this observation?

  a.

All of the RNase molecules have about 1% of their usual activity, due to changes to the organisation of disulphide bonds

  b.

Random formation of disulphide bonds mean about 1% of the RNase molecules are 100% active whereas 99% have no activity

  c.

Deprotonation of histidine in the active site of the enzyme means that only about 1% of the enzyme molecules are active

  d.

Deprotonation of histidine in the active site of the enzyme means that all of the enzyme molecules have 1% of their usual activity

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