Is the Conformational Ensemble of Alzheimer’s Aβ10-40 Peptide Force Field Dependent?
Fig 2
Aβ10-40 secondary structure in different force fields.
Total fractions of helix, turn, random coil, and β secondary structures for each of the five force fields probed in REMD simulations. All force fields predict dominance of turn and random coil conformations. C22* and OPLS-AA reveal moderate helix and β-structure propensities, respectively.