Oxygen-induced chromophore degradation in the photoswitchable red fluorescent protein rsCherry.

Reversibly switchable monomeric Cherry (rsCherry) is a photoswitchable variant of the red fluorescent protein mCherry. We report that this protein gradually and irreversibly loses its red fluorescence in the dark over a period of months at 4 °C and a few days at 37 °C. We also find that its ancestor, mCherry, undergoes a similar fluorescence loss but at a slower rate.

Probing Universal Protein Dynamics Using Hydrogen-Deuterium Exchange Mass Spectrometry-Derived Residue-Level Gibbs Free Energy.

Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is a powerful technique to monitor protein intrinsic dynamics. The technique provides high-resolution information on how protein intrinsic dynamics are altered in response to biological signals, such as ligand binding, oligomerization, or allosteric networks. However, identification, interpretation, and visualization of such events from HDX-MS data sets is challenging as these data sets consist of many individual data points collected across peptides, time points, and experimental conditions.

Structural Dynamics of the Functional Nonameric Type III Translocase Export Gate.

Type III protein secretion is widespread in Gram-negative pathogens. It comprises the injectisome with a surface-exposed needle and an inner membrane translocase. The translocase contains the SctRSTU export channel enveloped by the export gate subunit SctV that binds chaperone/exported clients and forms a putative ante-chamber.

Effect of point mutation on structure-function correlation of hemoglobin variants, HbE and HbD Punjab.

Hemoglobinopathies are examples of autosomal recessive disorders of human hemoglobin. Hemoglobin E (HbE) and Hemoglobin D Punjab (HbD Punjab) are two of the most common hemoglobin variants geographically spread across Asian continent. These two variants differ from normal human hemoglobin (HbA) at a single amino acid residue caused by the point mutation of β globin gene.

Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.

Bacterial secretory preproteins are translocated across the inner membrane post-translationally by the SecYEG-SecA translocase. Mature domain features and signal peptides maintain preproteins in kinetically trapped, largely soluble, folding intermediates. Some aggregation-prone preproteins require chaperones, like trigger factor (TF) and SecB, for solubility and/or targeting.

Comparative evaluation of herbal coccidiostat with chemotherapeutic coccidiostats on performance of broilers to control coccidiosis.

The objective of the present study was to investigate the comparative efficacy of recommended dose of selected anticoccidial drugs Salinomycin, Dinitolmide, while Cocciban at three dose levels on the performance of broilers. For this purpose, 420-day-old commercial male broiler chicks were randomly divided into 7 treatment groups with 10 replications of 6 birds each and reared in battery brooders up to 42 days of age. Groups were designated as uninfected unmedicated (T), infected unmedicated (T), Cocciban 500 g/ton and infected (T), Cocciban 750 g/ton and infected (T), Cocciban 1000 g/ton and infected (T), Salinomycin 500 g/ton and infected (T), and Dinitolmide and infected (T).

Understanding molecular features of aggregation-resistant tau conformer using oxidized monomer.

Background: Aggregation of tau into paired helical filament (PHF) is a hallmark of Alzheimer's disease (AD), and Cys-mediated disulfide bond formation plays a vital role in tau fibrillation. While intermolecular disulfide bond between Cys residues in microtubule-binding repeat (MTBR) region facilitates tau aggregation, intramolecular disulfide bond attenuates the same, though the molecular basis for such phenomenon remains obscure. Thus intramolecular disulfide-bonded tau monomer might be an excellent model to understand the unique features of aggregation-resistant tau conformer.

Effect of Cocciban herbal coccidiostats on hematobiochemical, fecal parameters and cecal histopathology of broiler chicken.

The objective of the present study was to investigate the comparative efficacy of recommended dose of selected anticoccidial drugs Salinomycin and Dinitolmide, while Cocciban at three dose levels on the hematobiochemical, fecal parameters and histopathology of broilers. For this purpose, 420-day-old commercial male broiler chicks were randomly divided into 7 treatment groups with 10 replications of 6 birds each and reared in battery brooders up to 42 days of age. Groups were designated as uninfected unmedicated (T), infected unmedicated (T), Cocciban 500 g/ton and infected (T), Cocciban 750 g/ton and infected (T), Cocciban 1000 g/ton and infected (T), Salinomycin 500 g/ton and infected (T), and Dinitolmide and infected (T).

Effect of ascorbic acid rich, micro-nutrient fortified supplement on the iron bioavailability of ferric pyrophosphate from a milk based beverage in Indian school children.

Background And Objectives: Nutritional anemia is a significant public health issue with 50-80% prevalence in Indian children. Fortification of food, specifically milk, with iron is a potential approach to increase dietary iron intake. Ferric pyrophosphate [Fe4(P2O7)3] is organoleptically neutral and is less soluble in acid medium and, further, has low bioavailability in milk.

Effect of altered solution conditions on tau conformational dynamics: Plausible implication on order propensity and aggregation.

Intrinsically disordered protein tau plays a central role in maintaining neuronal network by stabilizing microtubules in axon. Tau reportedly possesses random coil architecture, which is largely inert to alteration in solution conditions. However, the presence of transient compact conformers and residual structure has been evident from previous reports.

Adsorption Induced Changes of Human Hemoglobin on Ferric Pyrophosphate Nanoparticle Surface Probed by Isotope Exchange Mass Spectrometry: An Implication on Structure-Function Correlation.

In general, proteins in the biological system interact with nanoparticles (NPs) via adsorption on the particle surface. Understanding the adsorption at the molecular level is crucial to explore NP-protein interactions. The increasing concerns about the risk to human health on NP exposure have been explored through the discovery of a handful protein biomarkers and biochemical analysis.