One way to destabilise a folded protein structure is to change the solution conditions so that all the Asp and Glu side chains (and the C-terminus) become neutral, thus removing any stabilising ionic interactions and leaving a lot of Lys, Arg and His side chains (and the N-terminus) that repel each other.
Which of the following perturbations is most likely to destabilise a protein in this way?

Question

One way to destabilise a folded protein structure is to change the solution conditions so that all the Asp and Glu side chains (and the C-terminus) become neutral, thus removing any stabilising ionic interactions and leaving a lot of Lys, Arg and His side chains (and the N-terminus) that repel each other. 
 Which of the following perturbations is most likely to destabilise a protein in this way?

Answer

Adding a high concentration of guanidine

Answer

Changing the pH of the solution from 7 to 1 by adding hydrochloric acid

Answer

Increasing the solution to a high temperature (almost boiling)

Answer

Changing the pH of the solution from 7 to 13 by adding sodium hydroxide

Answer

Adding a high concentration of sodium dodecyl sulfate (SDS)

Crowdly

One way to destabilise a folded protein structure is to change the solution cond...

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