PPII propensity of multiple-guest amino acids in a proline-rich environment.
作者： Mahmoud Moradi , Volodymyr Babin , Celeste Sagui , Christopher Roland
DOI: 10.1021/JP203874F
关键词:
摘要: There has been considerable debate about the intrinsic PPII propensity of amino acid residues in denatured polypeptides. Experimentally, this scale is based on behavior guest placed middle proline-based hosts. We have used classical molecular dynamics simulations combined with replica-exchange methods to carry out a comprehensive analysis conformational equilibria host oligopeptides multiple acids including alanine, glutamine, valine, and asparagine. The tracked structural characteristics include secondary motifs Ramachandran angles cis/trans isomerization prolyl bonds. In agreement our recent study single guests, we did not observe an any multiple-guest setting. Instead, experimental results can be explained terms (i) steric restrictions imposed C-terminal that immediately followed by proline residue (ii) increase trans content bonds due presence residues. latter, found more guests added system, larger bonds, which effective peptide.
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