Convective heat transport in a porous wavy enclosure: Nonuniform multi-frequency heating with hybrid nanofluid and magnetic field.

This work investigates the dynamics of the hybrid nanofluidic convective heat transfer in a permeable thermal system under the influence of multifrequency heating and a magnetic field. The geometry comprises a wavy-walled cavity filled with a water-based hybrid nanoliquid (AlO-Cu-HO) in a saturated porous medium. The finite volume approach is applied to scrutinize the hydro-thermal characteristics resulting from bottom heating and side cooling, considering various flow-controlling parameters.

An application of artificial neural network (ANN) for comparative performance assessment of solar chimney (SC) plant for green energy production.

This study aims to optimize the power generation of a conventional Manzanares solar chimney (SC) plant through strategic modifications to the collector inlet height, chimney diameter, and chimney divergence. Employing a finite volume-based solver for numerical analysis, we systematically scrutinize influential geometric parameters, including collector height (h = 1.85 to 0.

Magneto-hydrothermal triple-convection in a W-shaped porous cavity containing oxytactic bacteria.

Bioconvective heat and mass transport phenomena have recently been the subject of interest in diverse fields of applications pertaining to the motion of fluids and their thermophysical properties. The transport processes in a system involving triple convective phenomena, irregular geometry, and boundary conditions constitute a complex phenomenon. This work aims to explore the mixed thermo-bioconvection of magnetically susceptible fluid containing copper nanoparticles and oxytactic bacteria in a novel W-shaped porous cavity.

Identification of Larval (Nematoda: Dioctophymatoidea) sp. from Bloch, 1793 by Morphological and Molecular Techniques.

Objective: This study aimed to identify the larval form of sp. isolated from the visceral organs of (Bloch, 1793) using morphological and molecular methods.

Methods: Fishes were collected from fish farms in Nadia and North 24 Paraganas for the collection of nematodes.

Bisphenol A-induced oxidative stress, hepatotoxicity and altered estrogen receptor expression in Labeo bata: impact on metabolic homeostasis and inflammatory response.

Bisphenol A (BPA), a weak estrogenic endocrine disruptor and a well-known plasticizer, has the potential to perturb diverse physiological functions; however, its impact on immune and metabolic function in aquatic vertebrates is relatively less understood. The present study aims to investigate the impact of BPA on hepatotoxicity, metabolic and immune parameters vis-à-vis estrogen receptor expression modulation in a freshwater teleost, Labeo bata (Cyprinidae, Cypriniformes). The 96-h median lethal concentration of BPA in L.

Study of Pathophysiological Effects of the Nematode Parasite Eustrongylides sp. on Freshwater Fish Channa punctatus by Hematology, Serum Biochemical, and Histological Studies.

Objective: The aim of this study was to study the pathophysiological effects on Channa punctatus due to the nematode parasite Eustrongylides sp.

Methods: A total of 250 fish were examined during the period January 2012-2014. Hematological, serum biochemical, histological, and scanning electron microscopic studies were performed on normal and infected hosts to study the effects caused by the nematode.

An anion induced multisignaling probe for Hg(2+) and its application for fish kidney and liver tissue imaging studies.

3',6'-Bis(diethylamino)-2-(pyridin-2-ylmethyl)spiro[isoindoline-1,9'-xanthen]-3-one () was synthesized for the selective fluorescence and colorimetric recognition of Hg(2+) at pH 6.0. In addition, was useful for imaging Hg(2+) in fish kidney and liver tissues using a fluorescence microscope.

A preliminary study on Oxya fuscovittata (Marschall) as an alternative nutrient supplement in the diets of Poecillia sphenops (Valenciennes).

Growth of the ornamental fish industry is being hindered by the scarcity of low cost feed; hence alternative protein supplements should be explored. In this context the present study aims to evaluate whether the grasshopper Oxya fuscovittata could be used as a supplement for fish meal in the diets of Poecillia sphenops, which is one of the most common ornamental fishes worldwide. The present work is divided into three phases: In the first phase proximate composition of the grasshopper is obtained and five diets are prepared where fish meal is gradually replaced by Oxya meal and named as control, D1, D2, D3 and D4.

Novel unfolding sequence of banana lectin: Folded, unfolded and natively unfolded-like monomeric states in guanidine hydrochloride.

The sequence of unfolding events of dimeric banana lectin (Banlec), as induced by guanidine hydrochloride (GdnHCl), has been investigated by size-exclusion HPLC, fluorescence, far-UV CD, low temperature phosphorescence and selective chemical modification. 8-Anilino-1-naphthalenesulfonate (ANS) binding indicates a structured unfolding intermediate which has been characterized as dissociated monomer by size-exclusion chromatography. Interestingly, the unfolding elution pattern reveals two distinct unfolded states.

Denaturation of bovine spleen galectin-1 in guanidine hydrochloride and fluoroalcohols: structural characterization and implications for protein folding.

Guanidine hydrochloride (GdnHCl)-induced unfolding of bovine spleen galectin-1 (Gal-1) exhibits three-state mechanism involving exclusive, structured tertiary monomer in 0.5 M GdnHCl. Gal-1 has one tryptophan residue (Trp 68) per subunit.

A comparative study of unfolding of Erythrina cristagalli Lectin in chemical denaturant and Fluoroalcohols.

The unfolding of dimeric Erythrina cristagalli lectin (ECL) has been investigated and compared under different denaturing conditions in presence of chemical denaturant, guanidine hydrochloride (GdnHCl) and fluoroalcohols, trifluoroethanol (TFE) and hexafluoroisopropanol (HFIP). The GdnHCl-induced unfolding exhibits three-state mechanism involving structured intermediate that corresponds to tertiary monomer. The intermediate has been characterized by 8- anilino-1-naphthalenesulfonate (ANS) binding, which shows ~ 30 fold increase in ANS fluorescence and selective chemical modification with N-bromosuccinimide when Trp 45 and Trp 207 are possibly oxidized.

Mercuric chloride induced toxicity responses in the olfactory epithelium of Labeo rohita (Hamilton): a light and electron microscopy study.

Bioaccumulation of mercury and histomorphological changes in the olfactory epithelium of Labeo rohita were investigated after exposing the fish to two sublethal concentrations of HgCl₂ (66 and 132 μg/L) for 15 and 30 days. Mercury deposition increased in the tissue significantly (p < 0.05) with dose- and duration-dependent manner.

Trifluoroethanol-induced conformational change of tetrameric and monomeric soybean agglutinin: role of structural organization and implication for protein folding and stability.

2,2,2-Trifuoroethanol (TFE)-induced conformational structure change of a β-sheet legume lectin, soybean agglutinin (SBA) has been investigated employing its exclusive structural forms in quaternary (tetramer) and tertiary (monomer) states, by far- and near-UV CD, FTIR, fluorescence, low temperature phosphorescence and chemical modification. Far-UV CD results show that, for SBA tetramer, native atypical β-conformation transforms to a highly α-helical structure, with the helical content reaching 57% in 95% TFE. For SBA monomer, atypical β-sheet first converts to typical β-sheet at low TFE concentration (10%), which then leads to a nonnative α-helix at higher TFE concentration.

Histopathological effects and bioaccumulation of mercury in the kidney of an Indian major carp, Labeo rohita (Hamilton).

The effect of mercuric chloride on the histo-morphology and bioaccumulation in the kidney of an Indian major carp, Labeo rohita (Hamilton) were examined after exposing the fish (15-20 cm) to three sublethal concentrations (0.033, 0.066 and 0.

Differing structural characteristics of molten globule intermediate of peanut lectin in urea and guanidine-HCl.

The structural characteristics of exclusive equilibrium molten globule-like intermediate formed during peanut lectin unfolding in urea and guanidine hydrochloride (GdnHCl) have been investigated by size-exclusion chromatography, circular dichroism, fluorescence, phosphorescence, and chemical modification. The elution behavior and 8-anilino-1-naphthalenesulfonate binding indicate a less compact tertiary structure in urea than in GdnHCl. Further, the urea-induced intermediate reveals perturbed, nonnative typical β-sheet conformation in contrast to native-like atypical β-structure in GdnHCl.

Localization and environment of tryptophans in different structural states of concanavalin A.

We have investigated the localization and environment of tryptophan residues in different quaternary and conformational states (tetrameric, dimeric, monomeric and unfolded) of metallized and demetallized concanavalin A (ConA) by selective chemical modification, fluorescence, and phosphorescence. ConA has four tryptophan residues (Trp 40, Trp 88, Trp 109 and Trp 182) per subunit. The pattern of oxidation by N-bromosuccinimide (NBS) shows that NBS modifies, in dimer, only Trp 182 which remains inaccessible in tetramer, two (Trp 88 along with Trp 182) in monomer, all four in unfolded form in presence of EDTA, and three (possibly Trp 40 along with Trp 88 and Trp 182) in unfolded form from native or remetallized ConA.

Pea lectin unfolding reveals a unique molten globule fragment chain.

Pea lectin (PSL) is a dimeric protein in which each subunit comprises two intertwined, post-translationally processed polypeptide chains--a long β-fragment and a short α-fragment. Using guanidine hydrochloride-induced denaturation, we have investigated and characterized the species obtained in the unfolding equilibrium of PSL by steady-state and time-resolved fluorescence, phosphorescence, and selective chemical modification. During unfolding, the fragment chains become separated, and the unfolding pattern reveals a β-fragment as intermediate that has the molten globule characteristics.

Organization and dynamics of tryptophan residues in tetrameric and monomeric soybean agglutinin: studies by steady-state and time-resolved fluorescence, phosphorescence and chemical modification.

We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies two tryptophans (Trp 60 and Trp 132) in tetramer, four (Trp 8, Trp 203 and previous two) in monomer, and all six (Trp 8, Trp 60, Trp 132, Trp 154, Trp 203 and Trp 226) in unfolded state. Utilizing wavelength-selective fluorescence approach, we have observed a red-edge excitation shift (REES) of 10 and 5 nm for tetramer and monomer, respectively.

Kinetic stability plays a dominant role in the denaturant-induced unfolding of Erythrina indica lectin.

The urea-induced denaturation of dimeric Erythrina indica lectin (EIL) has been studied at pH 7.2 under equilibrium and kinetic conditions in the temperature range of 40-55 degrees C. The structure of EIL is largely unaffected in this temperature range in absence of denaturant, and also in 8 M urea after incubation for 24 h at ambient temperature.

Quaternary association and reactivation of dimeric concanavalin A.

The reconstitution of dimeric concanavalin A (ConA) in terms of quaternary association and reactivation, after denaturation in urea, has been investigated using intrinsic fluorescence, 8-anilino-1-naphthalenesulfonate (ANS) binding, far-UV circular dichroism (CD), and an activity assay developed through a combination of affinity binding and the o-phthalaldehyde (OPA) procedure of protein estimation. The equilibrium denaturation of dimeric ConA in urea exhibits a biphasic unfolding pathway involving an intermediate with hydrophobic exposure, and the overall free energy of stabilization for the dimeric protein is obtained as 16.3 kcal mol(-1).

Kinetic analysis of subunit oligomerization of the legume lectin soybean agglutinin.

The reconstitution of soybean agglutinin (SBA), a tetrameric GalNAc/Gal-specific legume lectin, after denaturation in urea has been studied using fluorescence, far-UV CD, a hemagglutination assay, and chemical cross-linking with glutaraldehyde as a bifunctional reagent. The reconstituted protein exhibits similar quaternary structure and activity as of native lectin. The kinetics of subunit oligomerization has been determined from the cross-linking reaction of the reconstituting protein followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

Denaturant-induced equilibrium unfolding of concanavalin A is expressed by a three-state mechanism and provides an estimate of its protein stability.

The urea and guanidine hydrochloride (GdnHCl)-induced denaturation of tetrameric concanavalin A (ConA) at pH 7.2 has been studied by using intrinsic fluorescence, 8-anilino-1-naphthalenesulfonate (ANS) binding, far-UV circular dichroism (CD), and size-exclusion chromatography. The equilibrium denaturation pathway of ConA, as monitored by steady state fluorescence, exhibits a three-state mechanism involving an intermediate state, which has been characterized as a structured monomer of the protein by ANS binding, far-UV CD and gel filtration size analysis.