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. 2017 Nov 11;46(1):324–335. doi: 10.1093/nar/gkx1087

Figure 3.

Figure 3.

Molecular dynamic simulations of the NTA peptide. Selected conformations are shown, drawn to their calculated cross section in the distribution. The N-terminus of each structures is labeled. The sharp peak at 509 Å2 shows that the N-terminal eight residues of B25 is exposed to the solution. This feature was induced by simulating heating of the peptide to cause the unfolding of the peptide.