bioRxiv Subject Collection: Biophysics
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Ionic strength modulates structural disorder and protein oligomerization in the marginally disordered Phd transcription factor
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https://www.biorxiv.org/content/10.64898/2026.04.15.718675v1?rss=1
2026-04-17doi:10.64898/2026.04.15.718675Cold Spring Harbor Laboratory2026-04-17
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Redox-Triggered Coupling Network Mediates Long-Range Energy Trans-duction in Respiratory Complex I
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https://www.biorxiv.org/content/10.64898/2026.04.14.716442v1?rss=1
200 [A]) proton-coupled electron transfer process. To elucidate the molecular principles underlying this intricate action-at-a-distance effect, we combine here multiscale quantum/classical (QM/MM) simulations with site-directed mutagenesis, proteoliposome experiments, and cryo-electron microscopy (cryo-EM). We find that quinol binding at a distinct site within a local membrane cavity, triggers a long-range protonation cascade over water-mediated proton wires along a conserved carboxylate pathway (E-channel). We identify a central mechanical switch point, comprising the conserved Tyr156^H, the mutation of which impedes conformational changes along conserved loops, but not the proton transfer reaction itself. Using our integrative multi-disciplinary approach, we reveal central coupling sites along the redox-driven proton transport process mediating energy conversion in Complex I, and illustrate the power of theory-guided experiments.
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Ratiometric Quantification of Dissolved Molecular Oxygen in Microplates for Biochemical Assays Using Palladium Porphyrin Photoluminescence
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https://www.biorxiv.org/content/10.64898/2026.04.15.718663v1?rss=1
2026-04-17doi:10.64898/2026.04.15.718663Cold Spring Harbor Laboratory2026-04-17
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Dynamic-Structure Redesign of Calmodulin Reveals Mechanistic Constraints on Ryr2 Regulation
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https://www.biorxiv.org/content/10.64898/2026.04.14.717973v1?rss=1
2026-04-17doi:10.64898/2026.04.14.717973Cold Spring Harbor Laboratory2026-04-17
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A robust workflow for 3D imaging of human mitochondria using cryo-electron tomography
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https://www.biorxiv.org/content/10.64898/2026.04.16.717704v1?rss=1
2026-04-17doi:10.64898/2026.04.16.717704Cold Spring Harbor Laboratory2026-04-17
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Proteome-wide identification and modeling of interactions between transactivation domains and arginine-glycine-rich regions
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https://www.biorxiv.org/content/10.64898/2026.04.13.717676v1?rss=1
2026-04-16doi:10.64898/2026.04.13.717676Cold Spring Harbor Laboratory2026-04-16
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Mechanistic insights into the association and activation of the SARS-CoV-2 2'-O-Methyltransferase (NSP16)
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https://www.biorxiv.org/content/10.64898/2026.04.15.718757v1?rss=1
2026-04-16doi:10.64898/2026.04.15.718757Cold Spring Harbor Laboratory2026-04-16
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Topological defects and coherent myocardial chirality shape torsional heart contraction
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https://www.biorxiv.org/content/10.64898/2026.04.13.718243v1?rss=1
2026-04-16doi:10.64898/2026.04.13.718243Cold Spring Harbor Laboratory2026-04-16
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The dynamic and heterogeneous structure of the non-canonical inflammasome
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https://www.biorxiv.org/content/10.64898/2026.04.15.718739v1?rss=1
2026-04-16doi:10.64898/2026.04.15.718739Cold Spring Harbor Laboratory2026-04-16
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Biomolecular condensates provide a unique environment for redox-mediated protein crosslinking
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https://www.biorxiv.org/content/10.64898/2026.04.14.718453v1?rss=1
2026-04-16doi:10.64898/2026.04.14.718453Cold Spring Harbor Laboratory2026-04-16
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Differential effects of α-Synuclein monomers and seeds on the material properties of Tau condensates
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https://www.biorxiv.org/content/10.64898/2026.04.14.718443v1?rss=1
2026-04-16doi:10.64898/2026.04.14.718443Cold Spring Harbor Laboratory2026-04-16
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Asymmetric Hydration and Protonation Switching of Dual Aspartates Drive Flagellar Rotation
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https://www.biorxiv.org/content/10.64898/2026.04.14.718414v1?rss=1
2026-04-16doi:10.64898/2026.04.14.718414Cold Spring Harbor Laboratory2026-04-16
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Quantitative and mutational analysis of soluble HIV-1 Vpu and calmodulin interactions
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https://www.biorxiv.org/content/10.64898/2026.04.15.718738v1?rss=1
2026-04-16doi:10.64898/2026.04.15.718738Cold Spring Harbor Laboratory2026-04-16
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Protein entanglement misfolding determines divergent fates: proteasomal degradation or persistence in near-native misfolded states
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https://www.biorxiv.org/content/10.64898/2026.04.15.718748v1?rss=1
2026-04-16doi:10.64898/2026.04.15.718748Cold Spring Harbor Laboratory2026-04-16
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Influence of Lipomannan and Lipoarabinomannan Concentration on Mycobacterial Inner Membranes Characterized by All-atom Simulations
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https://www.biorxiv.org/content/10.64898/2026.04.15.718817v1?rss=1
2026-04-16doi:10.64898/2026.04.15.718817Cold Spring Harbor Laboratory2026-04-16
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Resolving the Activation Mechanism of the Human 20S Proteasome
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https://www.biorxiv.org/content/10.64898/2026.04.13.718244v1?rss=1
2026-04-15doi:10.64898/2026.04.13.718244Cold Spring Harbor Laboratory2026-04-15
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Heterotrimeric G proteins exhibit subtype-specific mobility differences in live cells
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https://www.biorxiv.org/content/10.64898/2026.04.13.718213v1?rss=1
2026-04-15doi:10.64898/2026.04.13.718213Cold Spring Harbor Laboratory2026-04-15
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Atomic structure and dynamics of the mechanosensitive channel MscL from E. coli by cryo-EM and solid-state NMR
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https://www.biorxiv.org/content/10.64898/2026.04.14.718163v1?rss=1
2026-04-15doi:10.64898/2026.04.14.718163Cold Spring Harbor Laboratory2026-04-15
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Far-from-equilibrium assembly of multimers through DNA-based catalytic templating
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https://www.biorxiv.org/content/10.64898/2026.04.13.718267v1?rss=1
2026-04-15doi:10.64898/2026.04.13.718267Cold Spring Harbor Laboratory2026-04-15
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From Pixel to Wave: A Geometric Complementary Code for Hierarchical Pixel-Based Morphometry
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https://www.biorxiv.org/content/10.64898/2026.04.13.718311v1?rss=1
2026-04-15doi:10.64898/2026.04.13.718311Cold Spring Harbor Laboratory2026-04-15
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On-lamella super-resolution cryo-CLEM for cryo-ET enabled by vacuum-free ultra-stable cryogenic fluorescence microscopy
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https://www.biorxiv.org/content/10.64898/2026.04.14.717675v1?rss=1
2026-04-15doi:10.64898/2026.04.14.717675Cold Spring Harbor Laboratory2026-04-15
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Single-molecule imaging and tracking on clinical liquid biopsies reveals cancer biomarkers nanoscale organization and heterogeneity
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https://www.biorxiv.org/content/10.64898/2026.04.13.717683v1?rss=1
2026-04-15doi:10.64898/2026.04.13.717683Cold Spring Harbor Laboratory2026-04-15
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Multifractal Fluctuations in Electrogram Dynamics Distinguish Atrial Fibrillation Phenotype, Drug Response, and Imminent Termination: Implications for Mechanism and Treatment.
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https://www.biorxiv.org/content/10.64898/2026.04.12.718068v1?rss=1
1.4 million seconds of high-density bipolar electrograms from 106 patients (paroxysmal n{approx}52, non-paroxysmal n{approx}54) undergoing left atrial mapping with a 24-bipole HD-Grid catheter at standardized sites (RENEWAL AF-ANZCTR ACTRN12619001172190)). Multifractal analysis using the Wavelet Transform Modulus Maxima Method (WTMM) was applied to a burst-energy observable to derive log-normal multifractal parameters c (support dimension), c (spectrum location), and c2 (fluctuations). Hierarchical mixed-effects models accounted for channels nested within locations within patients. A flecainide sub-study (n=15) provided paired pre-/post-infusion recordings, and 27 spontaneous termination events in 15 patients were analysed using 60-s pre-termination windows. Spatial texture of c2 was quantified by variogram-derived correlation length and sill.
ResultsAF electrograms exhibited robust multifractality confirming multifractal fluctuations as an intrinsic property of AF. Non-paroxysmal AF showed significantly reduced fluctuations versus paroxysmal AF (c2: {beta}=-0.01, p=0.001), indicating a paradoxical loss of fluctuations with disease progression. Flecainide selectively increased fluctuations in paroxysmal AF ({Delta}c2 = +0.04, p<0.01; {Delta}c = +0.06, p<0.01) but had no significant effect on fluctuations (c2) in non-paroxysmal AF, revealing phenotype-dependent drug response. Immediately prior to spontaneous AF termination, fluctuations increased significantly compared with sustained AF (c2: 0.198 vs 0.181, p=0.024). Spatial variogram analysis revealed heterogenous patterns in paroxysmal AF, whereas non-paroxysmal AF displayed a homogenised, flattened fluctuations landscape.
ConclusionsAtrial fibrillation exhibits robust multifractal dynamics rather than random electrical activity. Reduced fluctuations characterizes non-paroxysmal AF, whereas higher fluctuations is observed in paroxysmal AF, during flecainide modulation, and immediately prior to spontaneous termination. These findings suggest that multifractal fluctuations (c2) reflects the dynamical state of AF and may serve as a quantitative biomarker of disease progression, pharmacologic responsiveness, and proximity to termination.
CONDENSED ABSTRACTTAtrial fibrillation (AF) exhibits multifractal electrogram fluctuations that vary with disease stage, pharmacologic responsiveness, and proximity to spontaneous termination. In this study, multifractal fluctuations (c2) was higher in paroxysmal than non-paroxysmal AF, increased selectively with flecainide in paroxysmal AF, and rose immediately before spontaneous termination. These findings identify c2 as a quantitative marker of AF progression, and imminent reorganization. Clinically, multifractal analysis may enhance intra-procedural assessment of AF phenotype, guide drug selection, and improve recognition of transitions toward sinus rhythm, and connects AF with concepts of criticality and phase transitions.
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Emergence of rigidity percolation and critical behavior in tunable protein condensates
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https://www.biorxiv.org/content/10.64898/2026.04.13.718064v1?rss=1
2026-04-14doi:10.64898/2026.04.13.718064Cold Spring Harbor Laboratory2026-04-14
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Escherichia coli K12 exhibits a ~50% longer lag phase, but no difference in log phase growth rate, under hypomagnetic conditions (19 nT)
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https://www.biorxiv.org/content/10.64898/2026.04.13.717819v1?rss=1
2026-04-14doi:10.64898/2026.04.13.717819Cold Spring Harbor Laboratory2026-04-14
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Quantifying Mg2+ dependence on conformational equilibrium in the two-state 7SK RNA stem-loop 3
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https://www.biorxiv.org/content/10.64898/2026.04.11.717930v1?rss=1
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org.highwire.dtl.DTLVardef@3da34forg.highwire.dtl.DTLVardef@acd221org.highwire.dtl.DTLVardef@178b71org.highwire.dtl.DTLVardef@1c3aad6_HPS_FORMAT_FIGEXP M_FIG C_FIG KEY POINTSO_LIAddition of Mg2+ shifts the SL3 two-state conformational equilibrium through preferential association with the SL3e state
C_LIO_LIMg2+ association stabilizes an A-form-like geometry in the SL3e upper stem
C_LIO_LIDMS reactivity patterns in MgCl2 titration experiments provide a signature for identifying A*C wobble base pairs
C_LIO_LIDMS-MaPseq mutation fraction perturbation data are correlated with NMR chemical shift perturbation data, validating chemical probing as a structural reporter
C_LI
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Mechanical interaction enables a collective mode of protocell proliferation
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https://www.biorxiv.org/content/10.64898/2026.04.11.717946v1?rss=1
2026-04-14doi:10.64898/2026.04.11.717946Cold Spring Harbor Laboratory2026-04-14
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Engineered Channel Asymmetry Extends Hydrogen-Bonding Networks for Proton Conduction
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https://www.biorxiv.org/content/10.64898/2026.04.11.717926v1?rss=1
2026-04-14doi:10.64898/2026.04.11.717926Cold Spring Harbor Laboratory2026-04-14
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Single-particle light scattering reveals the dynamic heterogeneity of biomolecular condensates
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https://www.biorxiv.org/content/10.64898/2026.04.10.717862v1?rss=1
2026-04-14doi:10.64898/2026.04.10.717862Cold Spring Harbor Laboratory2026-04-14
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Third Harmonic Generation Microscopy Reveals Structure and Mucus Dynamics in Human Airway Epithelium Models
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https://www.biorxiv.org/content/10.64898/2026.04.10.717621v1?rss=1
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org.highwire.dtl.DTLVardef@1de66e3org.highwire.dtl.DTLVardef@34fe90org.highwire.dtl.DTLVardef@134b595org.highwire.dtl.DTLVardef@17d896b_HPS_FORMAT_FIGEXP M_FIG For Table of Contents Only
C_FIG
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