The free energy surface (FES) of three Poly-Alanine peptides is exhaustively reconstructed by using metadynamics. A specific collective coordinate has been introduced to account for the hydration of the N- terminal region of alpha-helical conformations. Calculations suggest that Poly-Alanine peptides mainly populate unfolded states. Interestingly FESs exhibit different properties among peptides thereby providing some hints on factors determining the conformational preferences of short Poly-Alanine sequences. Overall the calculations evidence the efficiency of Metadynamics in exploring free energy surfaces of biological relevant molecules.
|Titolo:||Exploring the Free Energy Surface of Short Peptides by Using Metadynamics|
CAMILLONI, CARLO (Primo)
|Data di pubblicazione:||2008|
|Tipologia:||Book Part (author)|
|Appare nelle tipologie:||03 - Contributo in volume|