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. 2016 Jan 4;12(1):e1004686. doi: 10.1371/journal.pcbi.1004686

Fig 1. R h comparison to number of residues, N. Filled and open circles represent experimental R h for IDPs [23,2642] and folded proteins [22,45,46], respectively.

Fig 1

The solid line is the R h dependence on N estimated from simulations of randomly configured protein structures [22]. Stippled lines show R h for randomly configured structures with chain propensities for PP II (f PPII) from 0.1 to 1 in 0.1 increments. Every other stippled line is end-labeled by its f PPII value.