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. Author manuscript; available in PMC: 2014 Oct 3.
Published in final edited form as: J Phys Chem B. 2013 Sep 12;117(39):11448–11459. doi: 10.1021/jp402589x

Figure 7.

Figure 7

Evolution of structural parameter during all-atom MD simulations of micelle-bound αS. (a) Root-mean-square-deviation (rmsd) between C[α] coordinates of αS residues 2–92 relative to the starting structures. (b) Micelle eccentricities. (c) Number of lysine ε-NH3+ groups of αS within hydrogen bonding distance (≤ 3.5 Å) to SDS(SO4−) or SLAS(COO−). (d) Contents of helical (α-helix and 310-helix) and β-sheet (β-bridge and β-bulges) secondary structures. Secondary structure was classified with the program DSSP.71