Abstract
The C96 and AMBER95 force fields were compared with small model peptides Ac-(Ala)n-NMe (Ac = CH3CO, NMe = NHCH3, n=2 and 3) in vacuo and in TIP3P water by computing the free-energy profiles using multicanonical molecular dynamics method. The C96 force field is a modified version of the AMBER95 force field, which was adjusted to reproduce the energy difference between extended β- and constrained α-helical energies for the alanine tetrapeptide, obtained by the high level ab initio MO method. The slight modification resulted in a large difference in the free energy profiles. The C96 force field prefers relatively extended conformers, whereas the AMBER95 force field favors turn conformations. © 2000 John Wiley & Sons, Inc. J Comput Chem 21: 748–762, 2000
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