The Anfinsen experiment we discussed in our meetings showed that protein folding is encoded in the primary structure of a protein. Anfinsen did his experiment at a concentration of 1mg/mL. Choose from the answers below the one you believe represents best what would have ahppened if he used instead the physiological concentration of ribonuclease (~100mg/mL).

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Question restatement: The Anfinsen experiment showed that protein folding is encoded in the primary structure. He conducted the experiment at 1 mg/mL. What would likely happen if he used the physiological ribonuclease concentration (~100 mg/mL) instead?

Option 1: it is likely that higher protein concentrations would have made diffcult the full elimination of urea leading to aggregation
- Evaluation: This option aligns with biochemical principles. At higher protein concentrations, solution viscosity and intermolecular encounters increase, promoting aggregation as proteins attempt to refold after denaturant removal. If urea must be fully removed to allow folding, higher concentrations raise the chance that partially folded species interact and aggregate rather than reach a correct native state. This reflects the expected difficulty in achieving complete denaturation reversal and proper folding when proteins are crowded, thereby compromising the refolding efficiency.

Option 2: if the experiment at the higher concentration of ribonuclease were to be done in diluted conditions it would hav ebeen the same
- Evaluation: This path mixes variables (protein concentration and dilution). Even if later diluted, the initial high-concentration phase can promote aggregation that persists or seeds incorrect folding pathways. The outcome would not be simply “the same”; the high-concentration history could alter folding kinetics and aggregation propensity, making this option incorrect because it overlooks the dependence on concentration during the denaturation/refolding transition.

Option 3: Anfinsen would have found the same answer with either ribonuclease concentration
- Evaluation: This asserts concentration independence of the fundamental information encoded in the primary sequence. However, the experimental reality is that crowding and aggregation at high concentrations interfere with proper refolding. Therefore, this option contradicts established understanding that folding efficiency and aggregation risk depend on protein concentration, making it incorrect.

Option 4: higher ribonuclease is unlikely to affect the experiment in measurable ways
- Evaluation: This is inconsistent with the concept of macromolecular crowding and aggregation physics. Increasing concentration from 1 mg/mL to ~100 mg/mL substantially changes the solution environment, often enhancing intermolecular interactions and aggregation tendencies. Consequently, this option is not supported by known biophysical principles and is incorrect.

Overall, the reasoning highlights how elevated protein concentrations raise the likelihood of aggregation during attempts to refold after denaturation, thereby reducing the yield of correctly folded native protein and altering the interpretation of the folding information encoded in the primary sequence. The analysis contrasts each alternative by focusing on how concentration affects urea removal, folding kinetics, and aggregation pathways.

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