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These results show that the fold of the protein primarily determines backbone flexibility.
Compared to the large differences within the thermodynamic predictions, predictions of backbone flexibility are more conserved.
The predicted conservation of backbone flexibility is consistent with natural expectations.
The specific changes in barnase backbone flexibility are accompanied by increased phi/psi angle fluctuations.
This difference is attributed to the difference in the backbone flexibility of the two polymers.
We evaluate this model of backbone flexibility using three different tests.
Note that backbone flexibility is not exactly conserved; in fact there are many local differences within Fig. 8.
While backbone flexibility metrics are mostly conserved, cooperativity correlation (long-range couplings) also demonstrate considerable amount of variation.
The H-bond network explains the dichotomy between conservation within backbone flexibility and the lack of conservation within cooperativity correlation.
The observed conservation of the backbone flexibility is attributed to the similar H-bond networks within the secondary structure elements.
This is an indication that there is a most probable state that is sharply peaked around typical backbone flexibility characteristics.
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