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. 2012 Aug 8;103(3):558–566. doi: 10.1016/j.bpj.2012.07.002

Figure 5.

Figure 5

Role of the linker in CTD stability by MD simulations. (A–C) SAP scores of the truncated forms C101, C113, and C125 at 300 K (solid black lines) and 400 K (red dotted lines). The SAP score evaluates the surface hydrophobicity of a residue based on three-dimensional structures. Usually a residue with a high SAP score is highly prone to aggregation because it creates a hydrophobic locus on the protein surface. (D and E) The difference profiles of SAP scores at 300 and 400 K obtained by subtracting the scores of C113 (solid lines) and C125 (dotted lines) by those of C101. The residues responsible for CTD aggregation were characterized based on the following two criteria: i), a low SAP score in C101 and C113 but a high score in C125 at 300 K; ii), a high SAP score in C113 and C125 but a low score in C101 at 400 K.