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The presence of very low concentrations of guanidinium chloride (GdmCl) alters the tertiary structure of the monomeric heme-containing enzyme, horseradish peroxidase (HRP). The change in tertiary structure of the protein was reflected in the mean fluorescence lifetime of its single tryptophan residue, which increased from 2.3 +/- 0.1 ns in the native enzyme(More)
The presence of very low concentrations of the widely used denaturant urea induces structural changes in the monomeric heme-containing enzyme, horseradish peroxidase (HRP). Structural alterations in the protein were reflected in quenching studies of tryptophan fluorescence using the widely used quencher acrylamide. Stern-Volmer quenching constants measured(More)
This paper analyzes the relative efficacies of lipophilicity vis-à-vis topological indices in the correlation of the biological properties of four groups of bioactive molecules: alcohols, barbiturates, triazinones , and ketobemidones . Wiener number (W), information-theoretic topological parameters (IC, SIC, CIC, IWD , and IWD ), and molecular connectivity(More)
Glycation, a local covalent interaction, leads to alterations in secondary and tertiary structures of hemoglobin, the changes produced by fructose being more pronounced than those caused by glucose. The Stokes diameter of hemoglobin increases upon glycation from 7 to 14 nm and a concurrent inter-chain cross-linking and heme loss are also observed,(More)
Absorption, steady-state fluorescence, steady-state fluorescence anisotropy, and intrinsic and induced circular dichroism (CD) have been exploited to explore the binding of calf thymus DNA (ctDNA) with three cationic phenazinium dyes, viz., phenosafranin (PSF), safranin-T (ST), and safranin-O (SO). The absorption and fluorescence spectra of all the three(More)
Caseins are relatively small (molecular mass approximately 20 kDa), unstructured milk proteins of which the main components are referred to as alpha(s)-, beta- and kappa-casein. All three components lack a compact folded conformation, which can be ascribed to a combination of their low overall hydrophobicity and high net charge. Structural transitions of(More)
Fluorescence and circular dichroism spectroscopy were used to study the effect of two surfactants having oppositely charged head groups - cationic cetyltrimethyl ammonium bromide (CTAB) and anionic sodium dodecyl sulphate (SDS) - on the structure of the intrinsically unstructured proteins alpha s-, beta- and kappa-caseins. Although globular proteins are(More)
Interaction of the local anesthetic dibucaine with small unilamellar vesicles of dimyristoylphosphatidylcholine (DMPC) and dioleoyl phosphatidylcholine (DOPC) containing different mol percents of cholesterol has been studied by fluorescence spectroscopy. Fluorescence measurements on dibucaine in presence of phospholipid vesicles containing various amounts(More)
Expansion of a polyalanine stretch from 10 to 12-17 residues in the N-terminus of the protein PABP2 has been implicated in the genetically acquired disease oculopharyngeal muscular dystrophy, characterized by nuclear protein deposits. Here we report a correlation between the structural properties and cell toxicity of two peptides mimicking the N-terminal(More)