tailieunhanh - A hydrophobic spine stabilizes a surfaceexposed α-helix according to analysis of the solvent-accessible surface area
Most of hydrophilic and hydrophobic residues are thought to be exposed and buried in proteins, respectively. In contrast to the majority of the existing studies on protein folding characteristics using protein structures, in this study, our aim was to design predictors for estimating relative solvent accessibility (RSA) of amino acid residues to discover protein folding characteristics from sequences. |
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