Starch fine molecular structures are of essentially important in determining its pasting and retrogradation properties. In this study, 10 different starches from various botanical sources were selected to investigate the combined action of amylose and amylopectin molecules in determining the starch physicochemical properties. Correlation between starch structural parameters with the pasting and retrogradation properties showed that amylose and amylopectin CLDs do not affect these properties in isolation. Such as, the amount of amylose long chains and amylopectin short chains are both positively correlated with the melting temperatures and enthalpy of retrograded starches. Furthermore, relatively longer amylose short to medium chains can result in higher trough and breakdown viscosity, while higher amount of amylopectin medium to long chains result in higher peak viscosity. The results help a better understanding of the importance of amylose and amylopectin fine molecular structures in determining starch functional properties.Golgi Reassembly and Stacking Proteins (GRASPs), including GRASP65/GRASP55, were firstly found as stacking factors of Golgi cisternae. Their involvement in other processes, such as unconventional protein secretion (UPS), have been demonstrated, suggesting GRASPs act as interaction hubs. However, structural details governing GRASP functions are not understood thoroughly. Here, we explored the structural features of human cis-Golgi GRASP65 in aqueous solution and compared them with those from trans-Golgi GRASP55. Besides their distinct Golgi localization, GRASP65/55 also seem to be selectively recruited to mitosis-related events or to UPS. Despite preserving the monomeric form in solution seen for GRASP55, as inferred from our SEC-MALS and DLS data, GRASP65 exhibited higher intrinsic disorder and susceptibility to denaturant than GRASP55 (disorder prediction, urea denaturation and circular dichroism data). Moreover, spectroscopic and microscopic studies showed for GRASP65 the same temperature-dependent amorphous aggregation and time-dependent amyloid fibrillation at 37 °C seen for GRASP55. In the latter case, however, GRASP65 presented a lower aggregation rate than GRASP55. The present and previous data evidenced that intrinsic disorder and formation of higher-order oligomers, such as amyloid fibrils, are common features within GRASP family potentially impacting the protein’s participation in cell processes.Dinoflagellates are the dominant source of bioluminescence in coastal waters. The luminescence reaction involves the oxidation of luciferin by a luciferase enzyme, which only takes place at low pH. The pH-dependence has previously been linked to four conserved histidines. It has been suggested that their protonation might induce a conformational change in the enzyme, thereby allowing substrate access to the binding pocket. selleck kinase inhibitor Yet, the precise mechanism of luciferase activation has remained elusive. Here, we use computational tools to predict the open structure of the luciferase in Lingulodinium polyedra and to decipher the nature of the opening mechanism. Through accelerated molecular dynamics simulations, we demonstrate that the closed-open conformational change likely takes place via a tilt of the pH-regulatory helix-loop-helix domain. Moreover, we propose that the molecular basis for the transition is electrostatic repulsion between histidine-cation pairs, which destabilizes the closed conformation at low pH. Finally, by simulating truncated mutants, we show that eliminating the C-terminus alters the shape of the active site, effectively inactivating the luciferase.This work explores Electrochemical Impedance Spectroscopy (EIS) detection for a highly-sensitive quantification of prostate-specific antigen (PSA) in Faradaic (f-EIS) and non-Faradaic modes (nf-EIS). Immobilization of monoclonal antibody specific to PSA (anti-PSA) was performed using 1-ethyl-3-dimethylaminopropylcarbodiimide hydrochloride and N-hydroxysuccinimide crosslinking agents in order to conjugate carboxylic (-COOH) terminated group of 16-Mercaptoundecanoic acid with amine (-NH3+) on anti-PSA epitope. This approach offers simple and efficient approach to form a strong, covalently bound thiol-gold (SAu) for a reliable SAM layer formation. Studies on the topographic of pristine Au-IDE surface were performed by Scanning Electron Microscopy and Energy Dispersive X-ray Spectroscopy techniques, meanwhile a 3-dimensional optical surface profiler, Atomic Force Microscopy and X-ray Photoelectron Spectroscopy techniques were used to validate the successful functionalization steps on the sensor transducer surface. Detection of PSA in f-EIS mode was carried out by measuring the response in charge transfer resistance (Rct) and impedance change (Z), meanwhile in nf-EIS mode, the changes in device capacitance was monitored. In f-EIS mode, the sensor reveals a logarithmic detection of PSA in a range of 100 ng/ml down to 0.01 ng/ml in Phosphate Buffered Saline with a recorded sensitivity of 2.412 kΩ/log10 ([PSA] ng/ml) and the limit of detection (LOD) down to 0.01 ng/ml. The nf-EIS detection mode yields a logarithmic detection range of 5000 ng/ml down to 0.5 ng/ml, with a sensitivity of 8.570 nF/log10 ([PSA] ng/ml) and an LOD of 0.5 ng/ml. The developed bio-assay yields great device stability, specificity to PSA and repeatability of detection that would pave its way for the future development into portable lab-on-chip bio-sensing system.Biogenesis of iron-sulfur (FeS) clusters in an essential process in living organisms due to the critical role of FeS cluster proteins in myriad cell functions. During biogenesis of FeS clusters, multi-protein complexes are used to drive the mobilization and protection of reactive sulfur and iron intermediates, regulate assembly of various FeS clusters on an ATPase-dependent, multi-protein scaffold, and target nascent clusters to their downstream protein targets. The evolutionarily ancient sulfur formation (Suf) pathway for FeS cluster assembly is found in bacteria and archaea. In Escherichia coli, the Suf pathway functions as an emergency pathway under conditions of iron limitation or oxidative stress. In other pathogenic bacteria, such as Mycobacterium tuberculosis and Enterococcus faecalis, the Suf pathway is the sole source for FeS clusters and therefore is a potential target for the development of novel antibacterial compounds. Here we summarize the considerable progress that has been made in characterizing the first step of mobilization and protection of reactive sulfur carried out by the SufS-SufE or SufS-SufU complex, FeS cluster assembly on SufBC2D scaffold complexes, and the downstream trafficking of nascent FeS clusters to A-type carrier (ATC) proteins.