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. Author manuscript; available in PMC: 2015 Sep 22.
Published in final edited form as: J Phys Chem B. 2009 Mar 19;113(11):3565–3571. doi: 10.1021/jp809810z

Figure 7.

Figure 7

Structures of the Bcl-xL with three peptides for simulations at t=10 ns. (A: Bak-Bcl-xL system; B:HBS helix 2a-Bcl-xL system; C: HBS helix 2b-Bcl-xL system) Bcl-xL structures are shown in purple, residues in Bak from Gly572 to Gly575 and the corresponding cyclic rings in HBS helix 2a and HBS helix 2b are shown in green; residue Asp584 (KAC in HBS helix 2b) is shown in red, HBS helix 2b forms a Y shape and anchors at the hydrophobic surface of Bcl-xL. The rest Parts of the three inhibitive peptides are shown in yellow.