What is the entropy difference between $n$ free-floating amino acids and $n$ amino acids that have been translated into a protein?

Is there any known calculation for the (~ average) change in entropy between $n$ free-floating amino acids in a cell, at typical physiological concentrations, versus those same $n$ amino acids after they have been translated into a protein by the ribosome?

I imagine calculating the conformational entropy of a protein can be quite involved, so a simplified calculation for this is fine. In general, I would be satisfied with a rough order-of-magnitude answer, or even a bound.

There are several difficulties that I can see in performing this calculation. First, the $n$ amino acids that go into a given protein might not represent $n$ independent samples of free-floating amino acids, but have correlations between their spatial locations (i.e., if the ribosome sucks up amino acids faster than amino acids can diffuse across the cell). Second, there is a change in the excluded volume of the $n$ free-floating amino acids vs. the $n$ polymerized amino acids, which affects translational entropy of surrounding water.