A comparison of structural and evolutionary attributes of Escherichia coli and Thermus thermophilus small ribosomal subunits: signatures of thermal adaptation.

In Tables 2 and 3 , we see an interesting trend that although eleven mesophilic proteins exhibit higher sequence conservation at disordered regions (compared to the ordered regions), but only two of them (18%) exhibit significantly high conservation at D2O sites (compared to O2O sites).

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Only S17 protein (after exclusion of lowly conserved region) has a higher conservation in disorder-to-order transition than order-to-order transition; however, the difference is marginally significant.

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