bioRxiv Subject Collection: Biophysics
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This feed contains articles for bioRxiv Subject Collection "Biophysics"
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Simulation of cell-size systems at long timescales with flexible protein structures
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https://www.biorxiv.org/content/10.64898/2026.06.20.733545v1?rss=1
2026-06-22doi:10.64898/2026.06.20.733545Cold Spring Harbor Laboratory2026-06-22
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The Dilated Cardiomyopathy E525K β-Myosin Mutation Causes Hypocontractility in Cardiomyocytes Without Altering Crossbridge Cycling
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https://www.biorxiv.org/content/10.64898/2026.06.18.733270v1?rss=1
2026-06-22doi:10.64898/2026.06.18.733270Cold Spring Harbor Laboratory2026-06-22
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Single-molecule insights into DNA gyrase in live bacteria
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https://www.biorxiv.org/content/10.64898/2026.06.21.733238v1?rss=1
2026-06-22doi:10.64898/2026.06.21.733238Cold Spring Harbor Laboratory2026-06-22
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LTP-patterned electromagnetic stimulation induces NMDA receptor-dependent synaptic plasticity in cortical networks
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https://www.biorxiv.org/content/10.64898/2026.06.17.732958v1?rss=1
2026-06-22doi:10.64898/2026.06.17.732958Cold Spring Harbor Laboratory2026-06-22
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Buzzing Frequency Influences Pollen Release in Buzz-Pollinated Poricidal Anthers
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https://www.biorxiv.org/content/10.64898/2026.06.17.732968v1?rss=1
2026-06-22doi:10.64898/2026.06.17.732968Cold Spring Harbor Laboratory2026-06-22
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Cell division dynamics generate heterogeneous contact-mediated signaling outputs
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https://www.biorxiv.org/content/10.64898/2026.06.18.733180v1?rss=1
2026-06-22doi:10.64898/2026.06.18.733180Cold Spring Harbor Laboratory2026-06-22
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Mechanical tension expands the microtubule lattice stepwise and modulates kinesin-1 binding in an isoform-dependent manner
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https://www.biorxiv.org/content/10.64898/2026.06.17.732986v1?rss=1
= 10.6 pN, within the range of Fmin = 1.29 pN to Fmax = 22.3 pN - comparable to forces from one to three kinesin-1 motors. Within this force range, the binding rate of kinesin-1 isoform KIF5B decreased reversibly within seconds by ~20% and the dissociation rate increased by ~10%, reducing mean run length, that in extreme cases decreased by up to 46%. Substantial heterogeneity was also observed along individual microtubules, where distinct lattice regions responded differently to applied force, implying that lattice expansion is not always uniform. Consistent heterogeneity was observed in cells, where MAPs with competing conformational preferences assembled in non-overlapping patches along the same microtubule. A cooperatively-switching lattice Ising model based on tubulin conformational bistability, supported by dynamics simulations, quantitatively reproduces these observations with a critical switching force Fc = 8.5 pN, similar to established mechanosensory proteins such as talin and E-catenin. Strikingly, no significant effects were observed for KIF5C, revealing a kinesin isoform-dependent mechanoresponse. Together, these findings establish microtubules as mechanochemical signal transducers, converting mechanical forces into biochemical signals with the speed, spatial precision and sensitivity required for rapid cellular responses.
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Live-cell imaging of enhancer-promoter dynamics reveals transient contact-driven gene activation
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https://www.biorxiv.org/content/10.64898/2026.06.21.733446v1?rss=1
2026-06-21doi:10.64898/2026.06.21.733446Cold Spring Harbor Laboratory2026-06-21
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Mechanical Checkpoint for Cell Division in Three-Dimensional Microenvironments
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https://www.biorxiv.org/content/10.64898/2026.06.16.732593v1?rss=1
2026-06-21doi:10.64898/2026.06.16.732593Cold Spring Harbor Laboratory2026-06-21
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Artificial Intelligence Models for Classifying Wrist Ligament Injuries Using Synthetically-Generated Joint Proximity Maps from Finite Element Models
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https://www.biorxiv.org/content/10.64898/2026.06.17.733030v1?rss=1
2026-06-21doi:10.64898/2026.06.17.733030Cold Spring Harbor Laboratory2026-06-21
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Extending the osmophobic effect to protein side chains with a unified transfer model across osmolyte classes
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https://www.biorxiv.org/content/10.64898/2026.06.17.732849v1?rss=1
2026-06-21doi:10.64898/2026.06.17.732849Cold Spring Harbor Laboratory2026-06-21
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Revealing interactions between glutathione peroxidase 4 and phosphoinositides
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https://www.biorxiv.org/content/10.64898/2026.06.17.732910v1?rss=1
2026-06-21doi:10.64898/2026.06.17.732910Cold Spring Harbor Laboratory2026-06-21
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BioBrain: A Multi-Agent Framework for Natural Language Driven Quantitative Microscopy Data Analysis
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https://www.biorxiv.org/content/10.64898/2026.06.17.732700v1?rss=1
2026-06-21doi:10.64898/2026.06.17.732700Cold Spring Harbor Laboratory2026-06-21
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Cell-sized droplet interfaces reorganize protein secondary structures through confinement-enhanced membrane interactions
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https://www.biorxiv.org/content/10.64898/2026.06.17.732854v1?rss=1
2026-06-21doi:10.64898/2026.06.17.732854Cold Spring Harbor Laboratory2026-06-21
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Capillary bundling of microtubules by condensates
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https://www.biorxiv.org/content/10.64898/2026.06.19.733462v1?rss=1
2026-06-20doi:10.64898/2026.06.19.733462Cold Spring Harbor Laboratory2026-06-20
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CD8-mediated organization of the TCR-pMHC interface shapes its force response and dissociation pathways
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https://www.biorxiv.org/content/10.64898/2026.06.16.732622v1?rss=1
2026-06-20doi:10.64898/2026.06.16.732622Cold Spring Harbor Laboratory2026-06-20
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Vesicle Internalization Proceeds via a Morphological Phase Transition
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https://www.biorxiv.org/content/10.64898/2026.06.16.732530v1?rss=1
2026-06-20doi:10.64898/2026.06.16.732530Cold Spring Harbor Laboratory2026-06-20
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Dose-Dependent Softening of Bacterial Model Membranes by Structurally Distinct Antimicrobial Peptides: A Coarse-Grained Molecular Dynamics Study
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https://www.biorxiv.org/content/10.64898/2026.06.18.733300v1?rss=1
2026-06-20doi:10.64898/2026.06.18.733300Cold Spring Harbor Laboratory2026-06-20
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Defining reversible binding rates in 1D systems dependent on diffusion, density, and excluded volume
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https://www.biorxiv.org/content/10.64898/2026.06.18.733157v1?rss=1
2026-06-20doi:10.64898/2026.06.18.733157Cold Spring Harbor Laboratory2026-06-20
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Multiple routes to red-shifted chlorophyll d-based photosynthesis
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https://www.biorxiv.org/content/10.64898/2026.06.16.732656v1?rss=1
2026-06-20doi:10.64898/2026.06.16.732656Cold Spring Harbor Laboratory2026-06-20
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Viral RNAs as Dual Graphs: Extending the Motif Universe of RNAs
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https://www.biorxiv.org/content/10.64898/2026.06.20.733508v1?rss=1
2026-06-20doi:10.64898/2026.06.20.733508Cold Spring Harbor Laboratory2026-06-20
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Non-contact direct sensing of material properties of biomolecular condensate using Scanning Ionic Conductance Microscopy
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https://www.biorxiv.org/content/10.64898/2026.06.16.731580v1?rss=1
2026-06-20doi:10.64898/2026.06.16.731580Cold Spring Harbor Laboratory2026-06-20
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Remodeling of mRNA by eIF4F in human translation initiation
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https://www.biorxiv.org/content/10.64898/2026.06.19.733470v1?rss=1
2026-06-19doi:10.64898/2026.06.19.733470Cold Spring Harbor Laboratory2026-06-19
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Predicting Human mRNA Isoform Levels from Site-Specific Splicing Kinetics in silico
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https://www.biorxiv.org/content/10.64898/2026.06.16.732643v1?rss=1
2026-06-19doi:10.64898/2026.06.16.732643Cold Spring Harbor Laboratory2026-06-19
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Decoding Bispecific Antibody Developability: Design Rules and Predictive Models from a 160-Member Library
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https://www.biorxiv.org/content/10.64898/2026.06.15.732449v1?rss=1
2026-06-19doi:10.64898/2026.06.15.732449Cold Spring Harbor Laboratory2026-06-19
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Concealed Conduction Vulnerability in Scn1b Haploinsufficiency Emerges with Osmotic Stress
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https://www.biorxiv.org/content/10.64898/2026.06.15.732501v1?rss=1
2026-06-19doi:10.64898/2026.06.15.732501Cold Spring Harbor Laboratory2026-06-19
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Emergent Tissue Rheology in a 3D Mechanically Adaptive Viscoelastic Cell Network Model
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https://www.biorxiv.org/content/10.64898/2026.06.15.731174v1?rss=1
2026-06-19doi:10.64898/2026.06.15.731174Cold Spring Harbor Laboratory2026-06-19
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Siphoviridae phage tails co-enrich with ex vivo amyloids
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https://www.biorxiv.org/content/10.64898/2026.06.17.733002v1?rss=1
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Target DNA-Mediated Plasmonic Coupling and Assembly Kinetics of Gold Nanorods for Label-Free Nucleic Acid Detection
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https://www.biorxiv.org/content/10.64898/2026.06.16.732610v1?rss=1
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Exploring the Structural and Functional role of α,β-unsaturated Ketoesters as Anti-Staphylococcal Agents Targeting Glutathione Peroxidase
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https://www.biorxiv.org/content/10.64898/2026.06.16.732695v1?rss=1
2026-06-18doi:10.64898/2026.06.16.732695Cold Spring Harbor Laboratory2026-06-18