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. 2009 Feb 26;106(11):4095–4100. doi: 10.1073/pnas.0807299106

Fig. 3.

Fig. 3.

Distribution of positive (A) and negative charges (B), and residues (C) part of the N-/C-terminal helices around the NP. Distances are between Au surface and amino acid charged end groups (A and B) or Cα atoms (C), before MD when the protein structure is folded. Dashed lines: Average distance of BPS O atoms from NP surface (8 Å) and one Debye length (9.6 Å) away from BPS O at 0.1 M NaCl.