Imagine you purify apamin, the bee venom toxin with 2 disulfide bonds that we learned about in class. In order to better understand its properties, you treat it with urea and a high concentration of BME. You then remove most of the BME and allow the entire mixture to come to equilibrium in the dilute BME. Finally, you remove all of the urea and BME. Based on the results of Christian Anfinsen’s famous experiment, you would expect to observe that: a) Apamin would refold correctly with the correct arrangement of disulfide bonds so that it is 100% native b) Apamin’s disulfide bonds would form randomly, resulting in 1/105 of the protein molecules returning to their native structure. c) Apamin’s disulfide bonds would form randomly, resulting in 1/3 of the protein molecules returning to their native structure. d) None of the disulfide bonds would form, so the apamin would be inactive.
Imagine you purify apamin, the bee venom toxin with 2 disulfide bonds that we learned about in class. In order to better understand its properties, you treat it with urea and a high concentration of BME. You then remove most of the BME and allow the entire mixture to come to equilibrium in the dilute BME. Finally, you remove all of the urea and BME. Based on the results of Christian Anfinsen’s famous experiment, you would expect to observe that:
a) Apamin would refold correctly with the correct arrangement of disulfide bonds so that it is 100% native
b) Apamin’s disulfide bonds would form randomly, resulting in 1/105 of the protein molecules returning to their native structure.
c) Apamin’s disulfide bonds would form randomly, resulting in 1/3 of the protein molecules returning to their native structure.
d) None of the disulfide bonds would form, so the apamin would be inactive.
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