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Abstract :
[en] Calculating the quantity of information present in each step of the protein folding process suggests that the multistep approach requires less information than the one-step model. Quantitative analysis reveals that the amino acids present in the polypeptide chain do not carry enough information to accurately predict the values of the angles Φ and Ψ in folded proteins. This conclusion results from comparing the amount of information carried by amino acids with the quantity of information necessary to determine Φ and Ψ, taking the complete Ramachandran map as the conformational space. It is shown that the two-step model (comprising two stages, the ES and LS) requires less information, owing to the fact that the final predictions of the angles Φ and Ψ can be based on a preexisting ES structure. Analysis based on information theory points to particular zones of the Ramachandran map that appear to play an important role in the context of protein structure prediction.
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