"Hot cores" in proteins: comparative analysis of the apolar contact area in structures from hyper/thermophilic and mesophilic organisms.

A more detailed analysis on the structurally conserved regions [ 18 ] (SCRs; see methods section) of the structures composing dataset A and B indicated that, in both datasets, a number of hyperthermophilic proteins underwent a highly significant ( P ( t ) < 0.001) increase of the hydrophobic contact area of those residues composing the SCRs (Figure 3 ; Table 3 ).

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