Long MD simulations (100 ns) for the important model cyclopentapeptide
cyclo(
D-Pro
1-Ala
2-Ala
3-Ala
4-Ala
5) were performed in explicit DMSO solution using both OPLS-AA and AMBER03 force fields.Simulations revealed conformational transitions between two main conformers, a predominant one (population93-99%) and a minor conformer (population 0.4-6.7%). These results are in excellent agreement with 20experimental proton-proton distances estimated for this cyclopentapeptide. The previously discussed
![](/images/gifchars/gamma.gif)
-turn-like conformation for Ala
4 was present only in a minor conformer.