We investigate the physics underlying the presence of a quasicondensate in a nearly one dimensional, weakly interacting trapped atomic Bose gas. We show that a Hartree-Fock (mean-field) approach fails to predict the existence of the quasicondensate in the center of the cloud: the quasicondensate is generated by interaction-induced correlations between atoms and not by a saturation of the excited states. Numerical calculations based on Bogoliubov theory give an estimate of the crossover density in agreement with experimental results.
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http://dx.doi.org/10.1103/PhysRevLett.97.250403 | DOI Listing |
Sci Rep
January 2025
Computational Physics Key Laboratory of Sichuan Province, Yibin University, Yibin, China.
The potential energy curves, dipole moments and transition dipole moments of the 14 Λ-S states and 30 Ω states of TlBr cation were performed using the multi-reference configuration interaction method. The Davidson correction and spin-orbit coupling effects were also considered. The spectroscopic properties and transition properties of TlBr cation were reported at the first time.
View Article and Find Full Text PDFBiochimie
January 2025
Department of Biochemistry, School of Biology, M.V. Lomonosov Moscow State University; Department of Biochemistry and Regenerative Biomedicine Faculty of Basic Medicine, M.V. Lomonosov Moscow State University. Electronic address:
BAG3 is a universal adapter protein involved in various cellular processes, including the regulation of apoptosis, chaperone-assisted selective autophagy, and heat shock protein function. The interaction between small heat shock proteins (sHsps) and their α-crystallin domains (Acds) with full-length BAG3 protein and its IPV domain was analyzed using size-exclusion chromatography, native gel electrophoresis, and chemical cross-linking. HspB7 and the 3D mutant of HspB1 (which mimics phosphorylation) showed no interaction, HspB6 weakly interacted, and HspB8 strongly interacted with full-length BAG3.
View Article and Find Full Text PDFEur J Med Chem
January 2025
Innovation Research Institute of Traditional Chinese Medicine, Shandong University of Traditional Chinese Medicine, Jinan, 250355, China. Electronic address:
Intravenously administered nanoparticles (NPs) often bind with plasma proteins, forming the protein corona that promotes rapid systemic clearance, a primary challenge in nanomedicine. In this study, we developed a pH- and GSH-sensitive "stealth" nanodelivery system, PTX@NPs-aPD1-IL, for sequential drug release. By using a biocompatible choline-based ionic liquid (IL) as the coating for NPs, the interaction and adsorption of NPs with serum proteins were reduced, achieving targeted delivery to the lung organ and increasing drug accumulation.
View Article and Find Full Text PDFChem Sci
January 2025
School of Materials and Energy, University of Electronic Science and Technology of China Chengdu 611731 China
Silicon (Si) is considered a promising anode material for next-generation lithium-ion batteries due to its high theoretical specific capacity and earth-abundancy. However, challenges such as significant volume expansion, unstable solid electrolyte interphase (SEI) formation in incompatible electrolytes, and slow lithium-ion transport lead to its poor cycling and rate performance. In this work, it is demonstrated that superior cyclability and rate capability of Si anodes can be achieved using ethyl fluoroacetate (EFA) and fluoroethylene carbonate (FEC) solvents with low binding energy with Li but with sufficiently high relative dielectric constants.
View Article and Find Full Text PDFChembiochem
January 2025
Institute for Drug Discovery, University of Leipzig, Brüderstr. 34, 04103, Leipzig, Germany.
Recent advances in computational methods like AlphaFold have transformed structural biology, enabling accurate modeling of protein complexes and driving applications in drug discovery and protein engineering. However, predicting the structure of systems involving weak, transient, or dynamic interactions, or of complexes with disordered regions, remains challenging. Nuclear Magnetic Resonance (NMR) spectroscopy offers atomic-level insights into biomolecular complexes, even in weakly interacting and dynamic systems.
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