We show that spatial quenched disorder affects polar active matter in ways more complex and far reaching than heretofore believed. Using simulations of the 2D Vicsek model subjected to random couplings or a disordered scattering field, we find in particular that ergodicity is lost in the ordered phase, the nature of which we show to depend qualitatively on the type of quenched disorder: for random couplings, it remains long-range ordered, but qualitatively different from the pure (disorderless) case. For random scatterers, polar order varies with system size but we find strong non-self-averaging, with sample-to-sample fluctuations dominating asymptotically, which prevents us from elucidating the asymptotic status of order.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1103/PhysRevLett.126.178001 | DOI Listing |
Biomolecules
January 2025
Department of Neurology, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University, 40225 Düsseldorf, Germany.
Proteomics accelerates diagnosis and research of muscular diseases by enabling the robust analysis of proteins relevant for the manifestation of neuromuscular diseases in the following aspects: (i) evaluation of the effect of genetic variants on the corresponding protein, (ii) prediction of the underlying genetic defect based on the proteomic signature of muscle biopsies, (iii) analysis of pathophysiologies underlying different entities of muscular diseases, key for the definition of new intervention concepts, and (iv) patient stratification according to biochemical fingerprints as well as (v) monitoring the success of therapeutic interventions. This review presents-also through exemplary case studies-the various advantages of mass proteomics in the investigation of genetic muscle diseases, discusses technical limitations, and provides an outlook on possible future application concepts. Hence, proteomics is an excellent large-scale analytical tool for the diagnostic workup of (hereditary) muscle diseases and warrants systematic profiling of underlying pathophysiological processes.
View Article and Find Full Text PDFBiosensors (Basel)
January 2025
School of Biomedical Sciences and Engineering, Koç University, 34450 Istanbul, Turkey.
Human monkeypox (Mpox) is a zoonotic disease caused by the Monkeypox virus (MPXV). As of 14 August 2024, the World Health Organization (WHO) has declared it a global health emergency. For Mpox, this was the second public health emergency of global significance in the past two years.
View Article and Find Full Text PDFSoft Matter
January 2025
Department of Physics, Government College of Engineering and Textile Technology, 12 William Carey Road, Serampore, Hooghly-712201, India.
The theoretical study of instabilities, thermal fluctuations, and topological defects in the crystal-rotator-I-rotator-II (X-R-R) phase transitions of -alkanes has been conducted. First, we examine the nature of the R-R phase transition in nanoconfined alkanes. We propose that under confined conditions, the presence of quenched random orientational disorder makes the R phase unstable.
View Article and Find Full Text PDFACS Appl Bio Mater
January 2025
Department of Chemistry, Indian Institute of Technology Palakkad, Palakkad, Kerala 678 623, India.
The aggregation of proteins, peptides and amino acids has been a keen subject of interest owing to their implications in metabolic disorders. In this work, we investigated the self-aggregation of the unmodified aromatic amino acid l-tryptophan (Trp) into unusual spherical microstructures. Using fluorescence spectroscopy and field emission scanning electron microscopy (FE-SEM), we detail the time-dependent transformation of monomeric tryptophan into spherical aggregates with distinct fluorescence characteristics (λ = 345 nm, λ = 430 nm) compared to the monomer.
View Article and Find Full Text PDFBMC Chem
January 2025
Gene Regulation Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi, 110067, India.
Trimethylamine-N-oxide (TMAO) is gut microbiota-derived metabolite, plays a critical role in human health and diseases such as metabolic, cardiovascular, colorectal cancer and, neurological disorders. Binding interactions between TMAO and serum albumins are crucial to understand the impact of TMAO on disease mechanisms. However, detailed insights into the interaction mechanisms, preferred binding locations, and conformational changes in BSA upon binding TMAO are still unclear.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!