Conservation of Hydrophobic and Hydrophilic Residues in Four-Helix Bundle

The conservation of the hydrophobic and the hydrophilic residue sites obtained from 1000 designed sequences with the Z-score method for a four-helix bundle has been studied. The folding dynamic and thermodynamic features of the designed sequences and their different mutations are also studied. It is found that this conservation is related to the stability and the fast folding of the model proteins. Our results are consistent with the experimental results.