Distance of the predicted hydrogen bonds formed between interacting residues of HSA and PS.

<p>Distance of the predicted hydrogen bonds formed between interacting residues of HSA and PS.</p

Binding and thermodynamic parameters for the interaction between PS and HSA, studied at different temperatures, pH

<p>Binding and thermodynamic parameters for the interaction between PS and HSA, studied at different temperatures, pH</p

Fluorescence quench titration of HSA with increasing PS concentrations.

<p>[HSA] = 3 µM, [PS] = 0–22.5 µM with 1.5 µM intervals (1–16), λ_ex = 280 nm studied in 10 mM Tris-HCl buffer, pH 7.4, 25°C. Arrow depicts the blue shift in the emission maximum of HSA with increasing PS concentrations. Inset shows the decrease in the relative fluorescence intensity of HSA at 336 nm (FI_{336 nm}) with increasing PS/HSA molar ratios.</p

Characteristics of three-dimensional fluorescence spectra of native HSA and its complexes with PS at pH 7.4, 25°C.

<p>Characteristics of three-dimensional fluorescence spectra of native HSA and its complexes with PS at pH 7.4, 25°C.</p

Analysis of fluorescence quenching data.

<p>(A) Stern–Volmer and (B) against plots of PS–HSA system at different temperatures. Inset of (B) shows the van’t Hoff plot for PS–HSA interaction.</p

3-D fluorescence spectral projections and corresponding contour maps of HSA and various PS–HSA complexes.

<p>(A and A′) Free HSA, (B and B′) 1∶1 PS–HSA, (C and C′) 2∶1 PS–HSA and (D and D′) 3∶1 PS–HSA. The spectra were recorded in 10 mM Tris-HCl buffer, pH 7.4, 25°C using a protein concentration of 3 µM.</p

Synchronous fluorescence spectra of HSA obtained in the absence and presence of increasing PS concentrations.

<p>[HSA] = 3 µM, [PS] = 0–22.5 µM with 1.5 µM intervals (1–16) studied in 10 mM Tris-HCl buffer, pH 7.4, 25°C. The difference between excitation and emission wavelengths (Δλ) was (A) 15 nm and (B) 60 nm. Arrows depict the position of the emission maximum of HSA in presence of increasing PS concentrations.</p

Cluster analysis of PS docking to binding sites I and II of HSA.

<p>The different crystal structures of HSA used in the analysis were (A) 1BM0, (B) 2BXD and (C) 2BXF. A total of 100 runs were performed for each binding locus.</p

Spectral overlap between the fluorescence spectrum of HSA and absorption spectrum of PS.

<p>Both spectra were recorded at 25°C in 10 mM Tris-HCl buffer, pH 7.4. The concentrations of HSA and PS were 3 µM each.</p

Model of PS docking to site I at subdomain IIA of HSA.

<p>Domain structure of HSA (I, red; II, blue and III, green), showing the binding orientation of the lowest docking energy conformation of PS. The zoomed-in view of the binding locus shows the ball-and-stick representation of the ligand and the side-chains of the protein residues (yellow) that form hydrogen bonds (green lines) with PS.</p