科研之友
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摘要
The right-handed alpha-helix is the dominant helical fold of alpha-peptides, whereas the left-handed 3(14)-helix is the dominant helical fold of beta-peptides. Using molecular dynamics simulations, the properties of alpha-helical alpha-peptides and 3(14)-helical beta-peptides with different C-terminal protonation states and in the solvents water and methanol are compared. The observed energetic and entropic differences can be traced to differences in the polarity of the solvent-accessible surface area and, in particular, the solute dipole moments, suggesting different reasons for their stability.
- 出版日期2010-11
