journal menu
![[Figure 5]](di5014fig5mag.jpg)
|
|
Figure 5
Dependence of the helical bending switch in the DHp dimer. (a, b, c) MD simulation of the DHp homodimer from the closed state of lpWalK for 40 ns. The original state (a) and a simulated state at ∼3 ns (c) of the DHp dimer are coloured purple and forest green. An intermediate state (b) is coloured grey. Helical bending angles are given below. PCA analysis of the MD simulation is shown for the first two PC planes. Blue indicates an assembly close to the state in (a), yellow for the state in (c) and grey for the state in (b). (d) Helical bending switch of an engineered DHp homodimer. The DHp dimer in state (c) is coloured forest green, and purple was used for rebuilding. A simulated state at 15 ns, coloured grey, was aligned with state (c). A rebuilt helical region (amino acids 372–382) taken from the opposite α1 is coloured red. The α1 back-shifting is highlighted with arrows. |
![[Figure 5]](di5014fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
