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
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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