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The nuclear pore complex (NPC) is the sole mediator of nucleocytoplasmic transport. Despite great advances in understanding its conserved core architecture, the peripheral regions can exhibit considerable variation within and between species. One such structure is the cage-like nuclear basket. Despite its crucial roles in mRNA surveillance and chromatin organization, an architectural understanding has remained elusive. Using in-cell cryo-electron tomography and subtomogram analysis, we explored the NPC's structural variations and the nuclear basket across fungi (yeast; S. cerevisiae), mammals (mouse; M. musculus), and protozoa (T. gondii). Using integrative structural modeling, we computed a model of the basket in yeast and mammals that revealed how a hub of nucleoporins (Nups) in the nuclear ring binds to basket-forming Mlp/Tpr proteins: the coiled-coil domains of Mlp/Tpr form the struts of the basket, while their unstructured termini constitute the basket distal densities, which potentially serve as a docking site for mRNA preprocessing before nucleocytoplasmic transport.

A novel tetra-peptide insertion was identified in Gag-p6 ALIX-binding region, which appeared in protease inhibitor failure Indian HIV-1C sequences (odds ratio=17.1, P

In this study, a phase change material (PCM)‐encapsulated packed‐bed thermal energy storage (PB‐TES) system is intended for Day‐round space heating in the winter. Solar concentric collectors act for day‐time heating and TES charging, while the stored energy can be used at night and intermediate time for space heating. A region‐wise techno‐economic analysis of PCM candidates is made to compare the costs and sizes of solar collectors and PB‐TES. A spherical capsule filled with sodium nitrite (NaNO2) and sodium nitrate (NaNO3) is numerically investigated during the PCM charging at constant thermal input. After complete liquefication, the charging time for NaNO2 and NaNO3 capsules is 3280 and 4300 s, respectively, holding the maximum stored energy of 733.4 KJ/kg at 285°C and 687.27 kJ/kg at 310.12°C, respectively. In addition, the stored exergy is obtained 238.78 and 234.74 kJ/kg for NaNO2 and NaNO3, respectively; however, the average exergetic effectiveness for NaNO2 and NaNO3 are 0.54 and 0.46. Despite the lower energy storage capacity (kJ/kg) of NaNO3, the PB‐TES volume is less with NaNO3 than with NaNO2 due to higher density. However, the average cost ($/tonne) of NaNO3 PCM is 50% higher than NaNO2. Subsequently, the thermal efficiency of the proposed system is estimated at 27.68% and 26.94% during day and night‐time operations. [ABSTRACT FROM AUTHOR]

The nuclear pore complex (NPC) is the sole mediator of nucleocytoplasmic transport. Despite great advances in understanding its conserved core architecture, the peripheral regions can exhibit considerable variation within and between species. One such structure is the cage-like nuclear basket. Despite its crucial roles in mRNA surveillance and chromatin organization, an architectural understanding has remained elusive. Using in-cell cryo-electron tomography and subtomogram analysis, we explored the NPC's structural variations and the nuclear basket across fungi (yeast; S. cerevisiae), mammals (mouse; M. musculus), and protozoa (T. gondii). Using integrative structural modeling, we computed a model of the basket in yeast and mammals that revealed how a hub of nucleoporins (Nups) in the nuclear ring binds to basket-forming Mlp/Tpr proteins: the coiled-coil domains of Mlp/Tpr form the struts of the basket, while their unstructured termini constitute the basket distal densities, which potentially serve as a docking site for mRNA preprocessing before nucleocytoplasmic transport., Competing Interests: Declaration of interests The authors declare no competing interests., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)

Biological processes are often mediated by complexes formed between proteins and various biomolecules. The 3D structures of such protein-biomolecule complexes provide insights into the molecular mechanism of their action. The structure of these complexes can be predicted by various computational methods. Choosing an appropriate method for modelling depends on the category of biomolecule that a protein interacts with and the availability of structural information about the protein and its interacting partner. We intend for the contents of this chapter to serve as a guide as to what software would be the most appropriate for the type of data at hand and the kind of 3D complex structure required. Particularly, we have dealt with protein-small molecule ligand, protein-peptide, protein-protein, and protein-nucleic acid interactions.Most, if not all, model building protocols perform some sampling and scoring. Typically, several alternate conformations and configurations of the interactors are sampled. Each such sample is then scored for optimization. To boost the confidence in these predicted models, their assessment using other independent scoring schemes besides the inbuilt/default ones would prove to be helpful. This chapter also lists such software and serves as a guide to gauge the fidelity of modelled structures of biomolecular complexes.