Rajiv Bhat

Jawaharlal Nehru University, New Delhi, NCT, India

Are you Rajiv Bhat?

Claim your profile

Publications (2)7.24 Total impact

  • [Show abstract] [Hide abstract]
    ABSTRACT: Effect of pH on the conformational behavior of Candida antartica lipase B (CaLB) has been monitored by spectroscopic and calorimetric studies. The results obtained from far and near-UV CD, intrinsic fluorescence and ANS binding studies indicate that CaLB exhibits the characteristic properties of a molten globule in acidic (protonated) condition at pH 1.4. The molten globule state retained about 67% of its secondary structure with a substantial loss of tertiary structure at pH 1.4. Moreover, equilibrium unfolding studies indicated that the 'molten-globule-like' state unfolds in a non-cooperative manner and is thermodynamically less stable than that of native state. The molten globule possessed a slightly higher Rh than its native state. DSC thermogram shows a high heat signal at pH 7.4, while low heat signal at pH 2.6, and suggests that CaLB is likely to have undergone structural changes during the thermal unfolding. However partially unfolded CaLB at pH 1.4 do not produce a DSC peak which proves the existence of molten globule state at pH 1.4 as supported by spectroscopic data. The Stokes radius of the MG state obtained by SEC experiments is found to be 33% larger than the native state, but essentially smaller than the denatured state.
    RSC Advances 02/2015; DOI:10.1039/C4RA17093H · 3.71 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: 1-naphthol (1N), 2-naphthol (2N) and 8-quinolinol (8H) are general water pollutants. 1N and 2N are the configurational enantiomers and 8H is isoelectronic to 1N and 2N. These pollutants when ingested are transported in the blood by proteins like human serum albumin (HSA). Binding of these pollutants to HSA has been explored to elucidate the specific selectivity of molecular recognition by this multiligand binding protein. The association constants (K(b)) of these pollutants to HSA were moderate (10(4)-10(5) M(-1)). The proximity of the ligands to HSA is also revealed by their average binding distance, r, which is estimated to be in the range of 4.39-5.37 nm. The binding free energy (ΔG) in each case remains effectively the same for each site because of enthalpy-entropy compensation (EEC). The difference observed between ΔC(p) (exp) and ΔC(p) (calc) are suggested to be caused by binding-induced flexibility changes in the HSA. Efforts are also made to elaborate the differences observed in binding isotherms obtained through multiple approaches of calorimetry, spectroscopy and bioinformatics. We suggest that difference in dissociation constants of pollutants by calorimetry, spectroscopic and computational approaches could correspond to occurrence of different set of populations of pollutants having different molecular characteristics in ground state and excited state. Furthermore, our observation of enhanced binding of pollutants (2N and 8H) in the presence of hemin signifies that ligands like hemin may enhance the storage period of these pollutants in blood that may even facilitate the ill effects of these pollutants.
    PLoS ONE 11/2011; 6(11):e26186. DOI:10.1371/journal.pone.0026186 · 3.53 Impact Factor