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Structural Determinants of Misfolding in Multidomain Proteins
Fig 8
Distribution of the “folding nucleus” location 
from the tandem dimer simulations (Table 1).
The 
of the (a) (SH3)2 (b) (SH2)2 (c) (TNfn3)2 and (d) (PDZ)2 are extracted at two different Q on the folding pathway (see individual figure legends for Q values). Note that the Q ∼ 0.5 corresponds to the structure with the first domain fully formed. The spread of contacts in sequence, within a given conformation, also becomes narrower with increasing Q (Fig B of S1 Text).
doi: https://doi.org/10.1371/journal.pcbi.1004933.g008