A compact and versatile tensile apparatus for polymer materials is designed and fabricated. Three distinct stretching modes are developed: constant speed, cyclic, and sinusoidal, with adjustable speeds ranging from 0.001 to 120 mm/s. To capture the true strain of the central region, a high-speed camera has been integrated into the apparatus. The temperature of the sample chamber is controlled by flowing air, enabling a homogeneous temperature in the range of RT ∼200 °C. The apparatus is particularly suitable for a synchrotron beamline. The structural evolution of natural rubber during sinusoidal stretching is investigated by in situ wide-angle x-ray scattering. Scattering patterns, force, clamp position, and sample images are saved simultaneously during stretching. Notably, the results reveal a sinusoidal variation in the crystallinity of crosslinked natural rubber when a sinusoidal strain was applied to the sample. The integration of advanced measurement techniques and controlled experimental conditions ensures the acquisition of reliable and accurate data, providing valuable insights into the structural evolution of materials under dynamic deformation conditions.
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http://dx.doi.org/10.1063/5.0202404 | DOI Listing |
J Mol Graph Model
December 2024
CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, 201 002, India. Electronic address:
Multi-scale models in which varying resolutions are considered in a single molecular dynamics simulation setup are gaining importance in integrative modeling. However, combining atomistic and coarse-grain resolutions, especially for coarse-grain force fields derived from top-down approaches, have not been well explored. In this study, we have implemented and tested a dual-resolution simulation approach to model globular proteins in atomistic detail (represented by the CHARMM36 model) with the surrounding solvent in Martini2 coarse-grain detail.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Univ Lyon, Université Claude Bernard Lyon 1, CNRS, LAGEPP UMR 5007, F-69100 Villeurbanne, France. Electronic address:
The immobilization of proteins onto clay surfaces has proven beneficial for pharmaceutical and environmental applications. This study examines the adsorption of sodium caseinate (Cas), an amphiphilic protein widely used in pharmaceutical formulations, onto sodium montmorillonite (Mt). Adsorption isotherms and kinetics were examined at two pHs, above and below Cas isoelectric point (IEP).
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
College of Chemistry and Material Science, Shandong Agricultural University, Taian 271018, Shandong, PR China; Key Laboratory of Agricultural Film Application of Ministry of Agriculture and Rural Affairs, Taian 271018, Shandong, PR China.
Polysaccharide-based films have received increasing attention as promising candidates for petrochemical plastics. However, they are highly brittle, poorly hydrophobic and without antibacterial activity, while current films used to address these issues often struggle to manage the balance between these properties. To achieve a balance of several performance indices of the films, functionalized dialdehyde cellulose nanocrystals (DCNCs) were prepared to activate pectin-based films.
View Article and Find Full Text PDFJ Colloid Interface Sci
December 2024
Department of Chemistry 'Ugo Schiff', University of Florence, via della Lastruccia 3-13, 50019 Sesto Fiorentino (FI), Italy. Electronic address:
The polyallylamine hydrochloride (PAH) polymer is here functionalized with branched and biocompatible polysaccharide dextran (DEX) molecules. Covalent conjugation of DEX to PAH has been achieved through a straightforward reductive amination approach, allowing for a controlled number of DEX chains per PAH polymer (PAH:DEX, n = 0.1, 0.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
December 2024
Department of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.
Optical imaging access to nanometer-level protein distributions in intact tissue is a highly sought-after goal, as it would provide visualization in physiologically relevant contexts. Under the unfavorable signal-to-background conditions of increased absorption and scattering of the excitation and fluorescence light in the complex tissue sample, superresolution fluorescence microscopy methods are severely challenged in attaining precise localization of molecules. We reasoned that the typical use of a confocal detection pinhole in MINFLUX nanoscopy, suppressing background and providing optical sectioning, should facilitate the detection and resolution of single fluorophores even amid scattering and optically challenging tissue environments.
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