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Magnetic force microscopy is a state-of-the-art high-resolution method of magnetic domain structure stray field investigation. Bulk uniaxial crystals with a branched domain structure are characterized by a stray field that changes rapidly with increasing distance from the sample surface. For such structures, it is most important to obtain magnetic force images at the lowest achievable tip-sample lift height z value. Present paper discusses an algorithm for experimental images processing. The algorithm results in modeled images at any lift height z, including the surface domain structure image (z = 0). It contains new information about additional domains and can be used for the most correct estimation of domain structure parameters and micromagnetic analysis. In addition, the spatial distribution of the tip-sample interaction force and energy can be calculated, and a statistical analysis of the structure complexity can be performed based on the results obtained.
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http://dx.doi.org/10.1016/j.micron.2025.103911 | DOI Listing |
J Am Coll Health
September 2025
Department of Epidemiology and Community Health, College of Health and Human Services, The University of North Carolina at Charlotte, Charlotte, North Carolina, USA.
Despite alarming rates of students' food insecurity in the US (41%), estimates may not be fully capturing experiences in university settings. Understanding students' food insecurity is a knowledge gap flagged amidst outstanding progress on food security measurement in household settings. This study investigated the domains shaping the experiences around food with implications for food insecurity among students.
View Article and Find Full Text PDFMol Biol Evol
September 2025
Department of Laboratory Medicine and Pathology, University of Washington Medical Center, Seattle, Washington, USA.
Human parainfluenza virus 2 (HPIV-2) and human parainfluenza virus 4 (HPIV-4) are significant but underappreciated respiratory pathogens, particularly among high-risk populations including children, the elderly, and immunocompromised individuals. In this study, we sequenced 101 HPIV-2 and HPIV-4 genomes from respiratory samples collected in western Washington State and performed comprehensive evolutionary analyses using both new and publicly available sequences. Phylogenetic and phylodynamic analyses revealed that both HPIV-2 and HPIV-4 evolve at significantly faster rates compared to mumps virus, a reference human orthorubulavirus.
View Article and Find Full Text PDFDisabil Rehabil Assist Technol
September 2025
School of Drama, Film and Television, Shenyang Conservatory of Music, Shenyang, China.
This study examines how choral singing functions as a mechanism for sustaining ritual practice and reinforcing cultural identity. By integrating perspectives from musicology, social psychology, and cognitive science, it explores how collective vocal performance supports emotional attunement, group cohesion, and symbolic memory in culturally diverse contexts. A mixed-methods approach was applied, combining ethnographic observation, survey-based data, and cognitive measures with AI-informed frameworks such as voice emotion recognition and neural synchrony modeling.
View Article and Find Full Text PDFSci Adv
September 2025
Division of Basic Sciences, Fred Hutchinson Cancer Center, Seattle, WA 98109, USA.
Integrins bind ligands between their alpha (α) and beta (β) subunits and transmit signals through conformational changes. Early in chordate evolution, some α subunits acquired an "inserted" (I) domain that expanded integrin's ligand-binding repertoire but obstructed the ancestral ligand pocket, seemingly blocking conventional integrin activation. Here, we compare cryo-electron microscopy structures of apo and ligand-bound states of the I domain-containing αEβ integrin and the I domain-lacking αβ integrin to illuminate how the I domain intrinsically mimics an extrinsic ligand to preserve integrin function.
View Article and Find Full Text PDFBioinformatics
September 2025
Biocomputation and Complex Systems Physics Institute (BIFI)-Joint Unit GBsC-CSIC, University of Zaragoza, Zaragoza, 50018, Spain.
Motivation: The stability of protein interfaces influences protein dynamics and unfolding cooperativity. Although in some cases the dynamics of proteins can be deduced from their topology, much of the stability of an interface is related to the complementarity of the interacting parts. It is also important to note that proteins that display non-cooperative unfolding cannot be rationally stabilized unless the regions that unfold first are known.
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