How well does molecular simulation reproduce environment-specific conformations of the intrinsically disordered peptides PLP, TP2 and ONEG?

A fairly significant β-ladder content was observed for the peptide in water (25.4 ± 3.5%) and the random coil content actually increased from 73.2 ± 2.7% to ∼91.0 ± 4.0% in the membrane-mimicking solvents, which is inconsistent with the experimental NMR and CD data ( Fig. 3 ). 6 There are no significant helical structures found in any of the simulations.

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