Steady State and Time Resolved Emission of TC in Various Solvents.

<p>(<b>A</b>) Fluorescence spectra of TC (25 µM) at 298 K in (1) water, (2) ethanol (EtOH), (3) isopropanol (iPrOH), (4) ethylene glycol (EG), (5) dimethylformamide (DMF), (6) dimethyl sulphoxide (DMSO); λ_exc = 370 nm; excitation and emission band pass = 10 nm and 5 nm respectively. (<b>B</b>) Fluorescence decay of TC (25 µM) at 298 K in (B) EtOH, iPr-OH, EG, DMF, DMSO; λexc = 370 nm; excitation and emission bandpass = 10 nm each.</p

Plot of φ (A) and <τ> (B) against (I) dielectric constant (ε), (II) solvent polarizability parameter (π*), (III) Hydrogen bond donating ability (α) of different solvents, (1) DMSO, (2) DMF, (3) EG, (4) EtOH, (5) i-PrOH.

<p>Plot of φ (A) and <τ> (B) against (I) dielectric constant (ε), (II) solvent polarizability parameter (π*), (III) Hydrogen bond donating ability (α) of different solvents, (1) DMSO, (2) DMF, (3) EG, (4) EtOH, (5) i-PrOH.</p

The plot of (A) (I) [F_∞ − F₀]/[F_x − F₀] against [BSA]⁻¹(II) (r−r_f)/R(r_b−r) against [BSA]; (B) (I) and (II) similar plot for HSA.

<p>The plot of (A) (I) [F_∞ − F₀]/[F_x − F₀] against [BSA]⁻¹(II) (r−r_f)/R(r_b−r) against [BSA]; (B) (I) and (II) similar plot for HSA.</p

The Changes in Accessible Surface Area (ΔASA)^a of the Residues of Serum Albumins after Complexed with Tetracycline.

a<p>ΔASA_i = ASAⁱ_HSA/BSA – ASAⁱ_{HSA/BSA – TC complex.}</p

Variation of (I) fluorescence quantum yield (φ).

<p>(II) fluorescence anisotropy (r); (III) singlet state average lifetime (τ) of TC (25 µM) in aqueous buffer with increasing concentration of serum albumins. (A) for BSA, (B) for HSA.</p

The Energy Transfer Efficiency and The Rate Constant of Protein-TC Complexes at 298 K.

a<p>Ref <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0060940#pone.0060940-Anand1" target="_blank">[66]</a>.</p>b<p>Considering the distance from indole N of Trp to O attached with 10-C of TC.</p

Distances and of Tryptophan Residues of Different Proteins from TC Changes in Accessible Surface Area (ΔASA) of Tryptophan Obtained by the Docking Studies.

<p>Distances and of Tryptophan Residues of Different Proteins from TC Changes in Accessible Surface Area (ΔASA) of Tryptophan Obtained by the Docking Studies.</p

Docked poses of serum albumin-TC complexes.

<p>(A) The surrounding amino acid residues of (I) BSA (II) HSA within 5 Å from TC. (B) Distances (in Å) obtained from docked poses of different Trp residue/s of (I) BSA (II) HSA from TC.</p

Phosphorescence Data for Wild-Type Serum Albumins and its Complex with TC in a 40% Ethylene Glycol Matrix at 77 K (λ_exc = 280 nm).

<p>Phosphorescence Data for Wild-Type Serum Albumins and its Complex with TC in a 40% Ethylene Glycol Matrix at 77 K (λ_exc = 280 nm).</p

Singlet State Lifetime and Quantum Yield of TC (25 µM) as a Function of Added Concentration of Serum Albumins with λ_ex = 370 nm at 298 K.

<p>Singlet State Lifetime and Quantum Yield of TC (25 µM) as a Function of Added Concentration of Serum Albumins with λ_ex = 370 nm at 298 K.</p