Cotranslational Protein Folding and Terminus Hydrophobicity

Figure 5

Showing that as the difference in mean terminus hydrophobicity increases, the difference between mean SAINT GDT_TS and reverse SAINT GDT_TS also increases. The curve shown is a lowess plot through the data based on 68 protein chains taken from [17]. Terminals comprised the first 10 (N-terminus) and last 10 (C-terminus) residues in the sequence. Mean hydrophobicity for each terminus was calculated using the Kyte-Doolittle scale [23]. Each protein was folded 1000 times using SAINT and reverse SAINT.