LOANONT-A RULE BASED ONTOLOGY FOR PERSONAL LOAN ELIGIBILITY EVALUATION

<p>In recent years, significant attention has been given to understand and implement banking solutions. The global competitive business environment and advancement in Information Technology and in particular internet technologies has facilitated the carrying out of banking activities outside the brick and mortar premise of the banks. Credit availing schemes are the core of the banking industry. Many agencies are working on it so as to make this facility hassle free for the customers and also to minimize the losses incurred by the banks in the form of bad debts. The challenge has been, and still is, to recognize, communicate and steadily improvise the banking solutions. The internet technologies are a potential candidates to overcome these challenges. The paper describes LoanOnt Ontology with the associated implementation toolset for creating an interoperable and sustainable personal loan calculation solution which would provide an intercommunication platform to facilitate integration and interoperation of information across interacting applications in banking scenarios.</p

Structural and Dynamical Insights into the Membrane-Bound α-Synuclein

<div><p>Membrane-induced disorder-to-helix transition of α-synuclein, a presynaptic protein, has been implicated in a number of important neuronal functions as well as in the etiology of Parkinson’s disease. In order to obtain structural insights of membrane-bound α-synuclein at the residue-specific resolution, we took advantage of the fact that the protein is devoid of tryptophan and incorporated single tryptophan at various residue positions along the sequence. These tryptophans were used as site-specific markers to characterize the structural and dynamical aspects of α-synuclein on the negatively charged small unilamellar lipid vesicles. An array of site-specific fluorescence readouts, such as the spectral-shift, quenching efficiency and anisotropy, allowed us to discern various features of the conformational rearrangements occurring at different locations of α-synuclein on the lipid membrane. In order to define the spatial localization of various regions of the protein near the membrane surface, we utilized a unique and sensitive indicator, namely, red-edge excitation shift (REES), which originates when a fluorophore is located in a highly ordered micro-environment. The extent of REES observed at different residue positions allowed us to directly identify the residues that are localized at the membrane-water interface comprising a thin (∼ 15 Å) layer of motionally restrained water molecules and enabled us to construct a dynamic hydration map of the protein. The combination of site-specific fluorescence readouts allowed us to unravel the intriguing molecular details of α-synuclein on the lipid membrane in a direct model-free fashion. Additionally, the combination of methodologies described here are capable of distinguishing subtle but important structural alterations of α-synuclein bound to different negatively charged lipids with varied head-group chemistry. We believe that the structural modulations of α-synuclein on the membrane could potentially be related to its physiological functions as well as to the onset of Parkinson’s diseases.</p></div

Fluorescence readouts of different Trp residues in the presence of SUVs derived from POPA (red), POPG (green) and POPS (Blue).

<p>Changes in (A) emission maxima (B) Stern-Volmer constants (C) Fluorescence anisotropy (D) REES. The standard error was estimated from at least three independent measurements.</p

Red-edge excitation shift (REES) of tryptophans in membrane-bound α-synuclein.

<p>(A) A cartoon of membrane bilayer depicting bulk (free) and restricted (biological) water. Fluorescence emission spectra of Trp 78 (B) and Trp 140 (C) varying the excitation wavelength (λ_ex) from 280 nm to 305 nm in the presence of POPG SUVs. (D) REES observed at different residue positions. The standard error was estimated from at least three independent measurements.</p

Distinct features of Trp variants located at different residues in the presence of POPG SUVs.

<p>(A) Normalized Trp fluorescence spectra showing spectral shift upon lipid binding. (B) Variation in emission maxima along the mutated residues. (C) Accessibility of Trp residues determined by Stern-Volmer constant (<i>K</i>_sv). (D) Fluorescence anisotropy of free IDP state (light grey) and membrane-bound form (dark grey). The standard error was estimated from at least three independent measurements.</p

Time-resolved fluorescence studies to monitor ultraslow hydration dynamics.

<p>(A) The nanosecond time-resolved decay of Trp 78 of α-synuclein in the presence of POPG SUVs showing progressive increase in the lifetime as a function of emission wavelength (IRF: instrument response time). (B) Time-resolved emission spectra showing gradual red-shift (in cm⁻¹) on the nanosecond timescale.</p

Amino acid sequence and mutational sites of α-synuclein.

<p>(A) The amino acid sequence showing negatively (red) and positively (blue) charged amino acids. The mutational sites for incorporating Trp are shown as underscored. (B) Various regions of the protein: N-terminal, NAC-domain and C-terminal. Trp positions are indicated in yellow.</p

A Label-Free and Ultrasensitive Prussian Blue-Based Dipstick Sensor for Bacterial and Biofilm Detection

Water and food contamination has become the major contributor to infections and deaths. However, rapid and sensitive bacterial detection still remains an unmet demand that has attracted widespread attention. Often water and food samples are sent out for laboratory testing to detect the presence of contamination, which is time-consuming and laborious. Herein, we have developed a highly sensitive, tenable, affordable, and robust (STAR) paper-based colorimetric dipstick sensor based on the principle of Prussian blue (PB) synthesis as an indicator of bacterial contamination. In the presence of bacteria, it leads to the formation of PB, a dye that acts as a colorimetric indicator. The intensity of the PB is the direct measure of the degree of contamination. The fabrication of the STAR dipstick sensor involves a simple and cost-effective process. The STAR dipstick sensor is ultrasensitive and can detect up to 101 CFU/mL of bacteria within minutes of contact with the test sample. The STAR dipstick sensor is fabricated using biodegradable components, which is speculated to facilitate quick and environmentally friendly degradation after each use. The sensor has been validated for its properties and capabilities at different pH to detect both Gram-positive and Gram-negative bacterial strains in real-time samples. The stability and degradation were also monitored. Comprehensively, the proposed STAR dipstick sensor can serve as a point-of-care device to detect bacterial contamination in a swift and sensitive manner

A Label-Free and Ultrasensitive Prussian Blue-Based Dipstick Sensor for Bacterial and Biofilm Detection

Water and food contamination has become the major contributor to infections and deaths. However, rapid and sensitive bacterial detection still remains an unmet demand that has attracted widespread attention. Often water and food samples are sent out for laboratory testing to detect the presence of contamination, which is time-consuming and laborious. Herein, we have developed a highly sensitive, tenable, affordable, and robust (STAR) paper-based colorimetric dipstick sensor based on the principle of Prussian blue (PB) synthesis as an indicator of bacterial contamination. In the presence of bacteria, it leads to the formation of PB, a dye that acts as a colorimetric indicator. The intensity of the PB is the direct measure of the degree of contamination. The fabrication of the STAR dipstick sensor involves a simple and cost-effective process. The STAR dipstick sensor is ultrasensitive and can detect up to 101 CFU/mL of bacteria within minutes of contact with the test sample. The STAR dipstick sensor is fabricated using biodegradable components, which is speculated to facilitate quick and environmentally friendly degradation after each use. The sensor has been validated for its properties and capabilities at different pH to detect both Gram-positive and Gram-negative bacterial strains in real-time samples. The stability and degradation were also monitored. Comprehensively, the proposed STAR dipstick sensor can serve as a point-of-care device to detect bacterial contamination in a swift and sensitive manner

Nanoscopic Amyloid Pores Formed via Stepwise Protein Assembly

Protein aggregation leading to various nanoscale assemblies is under scrutiny due to its implications in a broad range of human diseases. In the present study, we have used ovalbumin, a model non-inhibitory serpin, to elucidate the molecular events involved in amyloid assembly using a diverse array of spectroscopic and imaging tools such as fluorescence, laser Raman, circular dichroism spectroscopy, and atomic force microscopy (AFM). The AFM images revealed a progressive morphological transition from spherical oligomers to nanoscopic annular pores that further served as templates for higher-order supramolecular assembly into larger amyloid pores. Raman spectroscopic investigations illuminated in-depth molecular details into the secondary structural changes of the protein during amyloid assembly and pore formation. Additionally, Raman measurements indicated the presence of antiparallel β-sheets in the amyloid core. Overall, our studies revealed that the protein conformational switch in the context of the oligomers triggers the hierarchical assembly into nanoscopic amyloid pores. Our results will have broad implications in the structural characterization of amyloid pores derived from a variety of disease-related proteins