(7 of 15) Christian Anfinsen\'s experiment on the denaturation anc subsequent re

Question

(7 of 15) Christian Anfinsen's experiment on the denaturation anc subsequent refolding of ribonuclease has shaped the field of protein folding for sometime. From this experiment we have learned that: O the formation of the hydrophobic core is likely the single most important factor in stabilizing the structure of a globular protein. O the cell comes equipped with protein chaparones that do not direct protein folding but rather assist protein folding via a number of mechanisms. Othe correct formation of disulfide bonds in ribonuclease, and most proteins, requires a chaperone O protein folding is spontaneous and is not reliant upon a cellular apparatus to direct the formation of the correct native state.

Explanation / Answer

Last option is the correct answer. According to Anfinsen's experiment protein folding is thermodynamically most stable process with lowest in energy form. If a process is thermodynamicaaly stable it means the process is spontaneous. Although some proteins need some other protein for folding, these other proteins are known as chaperons and this disproves the Anfin'sens experiment.

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