Figures & data
Figure 1. Comparison of common structural indexes in PARP-1 in four different species. Note: H = Human, B = Bovine, M = Mouse, R = Rat.
![Figure 1. Comparison of common structural indexes in PARP-1 in four different species. Note: H = Human, B = Bovine, M = Mouse, R = Rat.](/cms/asset/1021d51d-66ad-442e-9600-eecc1316cdb3/tbeq_a_1726208_f0001_c.jpg)
Figure 6. Ramachandran plot for PARP4, Ramachandran contour plot depicting Φ and Ψ angles. Source: http://mordred.bioc.cam.ac.uk/∼rapper/rampage.php.
![Figure 6. Ramachandran plot for PARP4, Ramachandran contour plot depicting Φ and Ψ angles. Source: http://mordred.bioc.cam.ac.uk/∼rapper/rampage.php.](/cms/asset/5331039c-406a-4cbb-96e5-688dc161b9e6/tbeq_a_1726208_f0006_c.jpg)
Figure 10. Active site determination based on common structural motif that recognizes the NAD region of PARPs belonging to human, rat and mouse.
![Figure 10. Active site determination based on common structural motif that recognizes the NAD region of PARPs belonging to human, rat and mouse.](/cms/asset/6f47dd11-faa4-4836-9257-ccab15eb719b/tbeq_a_1726208_f0010_c.jpg)
Table 1. Comparative RMSD values of PARP1, PARP and PARP4 (°A).
Table 2. Catalytic sites from PARPs with the highest probability of interaction with NAD.
Figure 13. Electrophoresis (A) and chromatography (B) analysis of PARP1 and PARP2. Note: For electrophoresis analysis, 5 μg protein was loaded to gel.
![Figure 13. Electrophoresis (A) and chromatography (B) analysis of PARP1 and PARP2. Note: For electrophoresis analysis, 5 μg protein was loaded to gel.](/cms/asset/7d5bfc9a-9342-49e9-9331-1a3a2b3245e5/tbeq_a_1726208_f0013_c.jpg)
Figure 14. PARP1-NAD interaction was tested with thermal shift assay. Melting temperatures of PARP1-NAD interaction (Tm values).
![Figure 14. PARP1-NAD interaction was tested with thermal shift assay. Melting temperatures of PARP1-NAD interaction (Tm values).](/cms/asset/e85ae74e-97e4-46ea-b979-91cb97dd89d5/tbeq_a_1726208_f0014_c.jpg)