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The conformational properties of semiflexible active polar linear and ring phantom polymers are analyzed analytically to shed light on their dependence on activity. Special attention is paid to the influence of the implemented bond force for discrete and continuous polymer models. In detail, the Gaussian semiflexible polymer model and a model with a harmonic bond potential with finite bond length are considered. The studies reveal the immanent effects of the particular bond model on the polymer conformations as well as on the discrete or continuous representation. For continuum models, activity implies polymer end effects only, whereas for discrete models, all bonds can contribute to activity-dependent conformational changes. Ring polymers lack end effects; hence, continuous rings exhibit the same conformations as passive polymers. Similarly, the conformations of inextensible continuous polymers (Kratky-Porod worm-like chain) are activity-independent. These findings are in contrast to passive polymers, where a wide spectrum of bond potentials capture their generic features. Hence, this universality is broken by activity, and a model must be carefully selected to capture the characteristics observed in experiments.
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http://dx.doi.org/10.1063/5.0260802 | DOI Listing |
RSC Adv
September 2025
Departament de Química, Universitat Autònoma de Barcelona Bellaterra 08193 Barcelona Spain
Mammalian ALOX15 are allosteric enzymes but the mechanism of allosteric regulation remains a matter of discussion. Octyl (-(5-(1-indol-2-yl)-2-methoxyphenyl)sulfamoyl)carbamate inhibits the linoleate oxygenase activity of ALOX15 at nanomolar concentrations, but oxygenation of arachidonic acid is hardly affected. The mechanism of substrate selective inhibition suggests inter-monomer communication within the allosteric ALOX15 dimer complex, in which the inhibitor binding to monomer A induces conformational alterations in the structure of the active site of monomer B.
View Article and Find Full Text PDFJ Biomol NMR
September 2025
Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.
Biomolecular dynamics in the microsecond-to-millisecond (µs-ms) timescale are linked to various biological functions, such as enzyme catalysis, allosteric regulation, and ligand recognition. In solution state NMR, Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments are commonly used to probe µs-ms timescale motions, providing detailed kinetic, thermodynamic, and mechanistic information at the atomic level. For investigating conformational dynamics in high-molecular-weight biomolecules, methyl groups serve as ideal probes due to their favorable relaxation properties, and C CPMG relaxation dispersion is widely employed for characterizing dynamics in selectively CH-labeled samples.
View Article and Find Full Text PDFElife
September 2025
Chinese Academy of Medical Science Oxford Institute, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom.
Influenza virus neuraminidase (NA) is a crucial target for protective antibodies, yet the development of recombinant NA protein as a vaccine has been held back by instability and variable expression. We have taken a pragmatic approach to improving expression and stability of NA by grafting antigenic surface loops from low-expressing NA proteins onto the scaffold of high-expressing counterparts. The resulting hybrid proteins retained the antigenic properties of the loop donor while benefiting from the high-yield expression, stability, and tetrameric structure of the loop recipient.
View Article and Find Full Text PDFBiotech Histochem
September 2025
Laboratory of Veterinary Pathology, School of Veterinary Medicine, Azabu University, Kanagawa, Japan.
Amyloidosis is caused by the extracellular deposition of amyloid fibrils with a β-pleated sheet structure. Diagnosis typically relies on Congo red or Thioflavine T staining. Recently, DAPI (4',6-Diamidino-2-Phenylindole), which is a common nuclear fluorochrome, has been reported to stain amyloid.
View Article and Find Full Text PDFFood Res Int
November 2025
Fuzhou Institute of Oceanography, Minjiang University, Fuzhou 350108, China; Fujian Key Laboratory on Conservation and Sustainable Utilization of Marine Biodiversity, Minjiang University, Fuzhou, China. Electronic address:
This study employed high-pressure microfluidization (HPM) to facilitate the Maillard reaction between quinoa protein (QP) and dextran (DX), systematically examining the effects of various pressures on the conjugate's physicochemical properties. Fourier transform infrared spectroscopy confirmed the formation of QP-DX conjugates, characterized by a new peak at 1149 cm (covalent CN bond). Secondary and tertiary structure analyses revealed that HPM-assisted Maillard reaction partially unfolded QP molecules, enhancing conformational flexibility and interfacial properties.
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