Skip to main content
Advertisement
Browse Subject Areas
?

Click through the PLOS taxonomy to find articles in your field.

For more information about PLOS Subject Areas, click here.

< Back to Article

Table 1.

List of selected hit molecules and their docking score.

More »

Table 1 Expand

Fig 1.

Structural representation of docked compounds in the binding pocket of SIRT1.

(A) Cartoon representation of SIRT1 with Doxercalciferol (magenta) and Timiperone (cyan) along with the reference inhibitor Selisistat (green). (B) Surface potential view of SIRT1 binding pocket occupied by the selected compounds and Selisistat.

More »

Fig 1 Expand

Fig 2.

2D structural representation of SIRT1 residues interacting with (A) Doxercalciferol, (B) Timiperone, and (C) Selisistat.

More »

Fig 2 Expand

Table 2.

List of selected compounds and their biological properties calculated through PASS webserver.

Pa, probability to be active; Pi, probability to be inactive.

More »

Table 2 Expand

Fig 3.

Structural dynamics and compactness of SIRT1 upon Doxercalciferol and Timiperone binding as a function of time.

(A) RMSD plot of SIRT1 in complex with Doxercalciferol and Timiperone. (B) Residual fluctuations (RMSF) plot of SIRT1 before and after Doxercalciferol and Timiperone binding. (C) Time evolution of radius of gyration (Rg). (D) SASA plot of SIRT1 as a function of time.

More »

Fig 3 Expand

Fig 4.

Intramolecular hydrogen bonding.

(A) Time evolution and stability of hydrogen bonds (H-bonds) formed within 0.35 nm Intra-SIRT1 before and after Doxercalciferol and Timiperone binding. (B) The probability distribution function (PDF) of the H-Bonds for both the systems.

More »

Fig 4 Expand

Fig 5.

Intermolecular hydrogen bonding.

(A) The time evolution plot shows the formation of intermolecular hydrogen bonds between SIRT1 and Doxercalciferol. (B) The plot shows PDF of SIRT1 and Doxercalciferol hydrogen bonds. (C) Time evolution plot of hydrogen bonds between SIRT1 and Timiperone. (D) PDF plot of hydrogen bonds between SIRT1 and Timiperone.

More »

Fig 5 Expand

Fig 6.

Secondary structure dynamics of (A) free SIRT1, (B) SIRT1-Doxercalciferol, and (C) SIRT1-Timiperone. The secondary structure content in SIRT1 is the sum of α-helix, β-sheet, β-bridge, and turns.

More »

Fig 6 Expand

Fig 7.

Principal component analysis.

(A) 2D projections of trajectories on eigenvectors (EVs) showing conformational projections of SIRT1, SIRT1-Doxercalciferol and SIRT1-Timiperone (B) The time-evolution of projections of trajectories on both EVs.

More »

Fig 7 Expand

Fig 8.

The Gibbs free energy landscapes for (A) free SIRT1 (B) SIRT1-Doxercalciferol and Timiperone.

More »

Fig 8 Expand