journal menu
![[Figure 4]](mv5102fig4mag.jpg)
|
|
Figure 4
Secondary-structure content and thermal stability of NLRP14 PYD variants. (a) Wild-type NLRP14 PYD (pink) and NLRP14 PYD L84R (cyan) reveal a virtually identical CD spectrum, consistent with a nearly identical α-helical content in the open and closed conformation. (b) The thermal melting curve of the L84R mutant (cyan) is significantly shifted to higher temperatures compared with the wild-type PYD. This 17° shift corresponds to melting temperatures of 82.6 ± 1.3 and 65.6 ± 0.5°C for the L84R mutant and wild-type NLRP14 PYD, respectively. (c) The grey surface area corresponds to approximately 490 Å2 of hydrophobic contact area which becomes exposed upon transition from the closed six-helix bundle state (corresponding to the L84R mutant) to a (partially) extended α5/6 helix conformation (wild-type protein). |
![[Figure 4]](mv5102fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
