Question

Explain using the free energy considerations how proteins and RNA molecules evolved to stabilize their 3D-folds under high temperatures compared homologous proteins and RNA molecules evolving at lower temperatures (8 points) (Hint: comparative folding diagrams).

                                   

Answer 1

So, here’s the answer to your question.

To start with the first part of the question, the expansion of the base sequence actually requires the folding of RNA. For this process to happen there are methods such as chemical mapping, sequence comparison which are accompanied by the principles of thermodynamics. To find the RNA's that are new and those which are functional can be determined by the mixing of the of those functional RNA's that are noncoding because of which they are flexible to fold the free energies in comparison with other RNA's.

If the thermodynamics is the one single way to understand the folding, the chances of understanding the secondary structure from the sequence are possible.

There are other methods which involve basically three approaches

1. In order to determine the structures of lower free energies the structure with base pairing possibilities with color representation.

2. With the help of the stochastic sampling, the structures among the folding part will get samples in accordance with their chance or probability of occurring Here these sampled structures understand the chances of pairing the bases

3. In this method of approach, the structure with sequences of high probable pairs is assembled. The structures are otherwise called the Maximum expected accurate structures

So to answer the main part of the question that is a comparison, so the changes that occur in the composition of amino acids in accordance with low temperatures have not shown much of a difference in comparison with higher temperatures. But there is a prominent observation in the composition of amino acids of the proteins when compared between the prokaryotic organisms at low temperatures and to organisms that of the high temperatures

And the fact that mutations can also affect the speed of two different types of proteins that is the two state-like and non two sate like proteins. The reason for this is the modulations of association that aid the native state and also by strengthening specific non-native associations that are not present in the structure that is folded.

I hope this helps. Please do let me know if I can help you with anything.

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