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• W2050806147 abstract "Abstract The occurrence of cis imide bonds in proteins is much higher than that of cis amide bonds due to the unique properties of proline. In order to examine the relationship between the high occurrence of these cis imide bonds and the residues preceding the proline, we perform molecular dynamics simulations of trans - and cis - N -acetyl- N ′-methylamides of XaaPro dipeptides (AcXaaProNHMe). We investigate the conformational energies and structures of trans - and cis -AcXaa where Xaa has 12 amino acids in the vacuum state and 5 amino acids in the solution state. It is found that the occurrence of the cis imide bonds is strongly affected by the residue preceding the proline, and the dihedral angles (φ,ψ) of the backbone in AcXaaProNHMe are influenced by the configuration of the imide bond. We also find that the equilibrium properties of XaaPro in solution simulations are more similar to the statistics of X-ray crystallographic data than are those in vacuum simulations and solvation causes a remarkable change in the conformation of the pyrrolidine ring from the endo to the exo form." @default.
• W2050806147 created "2016-06-24" @default.
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• W2050806147 date "1994-07-01" @default.
• W2050806147 modified "2023-09-27" @default.
• W2050806147 title "Molecular dynamics simulations of trans- and cis-N-acetyl-N′-methylamides of XaaPro dipeptides" @default.
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• W2050806147 doi "https://doi.org/10.1016/0022-2860(94)08300-2" @default.
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