Stern-Volmer plot.

<p>Acrylamide quenching of native, denatured and pollutant complexed HSA (2 µM) at 37°C.</p

Dynamic light scattering of HSA-pollutant complex.

<p>Determination of hydrodynamic radii (<i>R</i>_h) of HSA in absence and presence of pollutants.</p

Acrylamide quenching results of HSA in absence and presence of pollutants.

<p>Acrylamide quenching results of HSA in absence and presence of pollutants.</p

Enzyme kinetics for HSA.

<p>(A) is the Michaeil-Menton equation based; (B) is the Lineweaver-Burk plots of reaction velocity versus substrate concentration for enzyme kinetics of HSA in absence and presence of pollutants (1∶5); (C) is the plot of % activity against pollutant concentrations at a fixed substrate and HSA concentration.</p

Difference in sequential unfolding of albumin (N) in absence and presence of pollutants.

<p>At mild temperature domain I and II separates and domain III melts out giving an expanded (E) conformation to the albumin. <i>i</i>_DII and <i>i</i>_DI corresponds to intermediates populated from the melting of domain II and I respectively and U is unfolded albumin.</p

Transition temperatures (T_m1 and T_{m 2}) and temperature mediated intermediates of HSA in absence and presence of pollutants (1∶5).

<p>Transition temperatures (T_m1 and T_{m 2}) and temperature mediated intermediates of HSA in absence and presence of pollutants (1∶5).</p

Structures.

<p>Pollutants (1N, 2N and 8H) and the substrate of HSA (nitrocefin).</p

Secondary structures of HSA in absence and presence of pollutants.

<p>Secondary structures of HSA in absence and presence of pollutants.</p

Enzyme kinetics parameters of HSA in absence and presence of pollutants (1∶5).

a<p>The data of enzyme kinetics for a true microbial β-lactamase using benzylpenicillin as substrate;</p>b<p>Acetylcholinesterase using acetylcholine as substrate is considered as an ideal enzyme;</p>c<p>The theoretical values for an ideal enzyme.</p

Thermal scan profiles of HSA in absence and presence of pollutants (1∶5) by CD.

<p>The values of (A) θ_{222 nm} for secondary structures and (B) θ_{263 nm} for tertiary structures were plotted against temperature. The insets are plots for the plus derivative of θ (mdeg) with respect to temperature (dθ/dT) versus temperature for the observation of fractional populations of domain specific intermediates.</p