388 papers
Biophysics sits at the fascinating intersection where the laws of physics meet the complexity of living systems. This field uses tools like light, electricity, and mechanical forces to decode how cells move, how proteins fold, and how our senses translate the world around us. Rather than just observing biology, biophysicists measure and model life to understand the fundamental machinery that powers every organism.
On Gist.Science, we make these discoveries accessible by curating the latest preprints directly from bioRxiv. Our team processes every new submission in this category, providing both clear, plain-language overviews and detailed technical summaries so readers of all backgrounds can grasp the cutting-edge science. Below are the most recent biophysics papers from bioRxiv, ready for you to explore.
This study demonstrates that the AI-based tool BioEmu can efficiently generate plausible conformational ensembles for membrane proteins like GlpG, capturing rare states and flexible domains at a fraction of the computational cost of traditional molecular dynamics simulations, though it does not fully replicate the entire landscape observed in physics-based modeling.
This study introduces a coupled Maxwell-electromagnetic cable framework that integrates FDTD solutions with extended membrane dynamics to demonstrate that classical quasi-static models significantly underestimate electromagnetic effects, revealing that magnetic induction and displacement currents critically alter action potential propagation speed, bifurcation transmission fidelity, and impedance matching in geometrically branched neuronal structures.
This study challenges the classical two-state allosteric paradigm by demonstrating that in yeast chorismate mutase, global conformational switching between T and R states is incidental to catalytic activity, which is instead governed by local features of the ground-state ensemble.
By mapping over 160,000 variants across five human kinases, this study reveals that while some allosteric sites are conserved, each kinase possesses a unique and divergent energetic architecture with distinct functional secondary sites, offering new opportunities for developing specific therapeutic inhibitors and activators.
This study reveals that RNA recognition by the tandem RRMs of the Sex-lethal protein is governed by a finely balanced, dynamic conformational ensemble shaped by transient interdomain interactions, where perturbations shifting this equilibrium in either direction compromise both binding affinity and sequence selectivity.
This study utilizes GPU-accelerated molecular dynamics simulations of a valency-limited stickers-and-spacers model to demonstrate that while heterogeneous nonspecific spacer interactions promote biomolecular condensation, they simultaneously disrupt the internal organization and compositional robustness of the resulting condensates, revealing a fundamental tradeoff between phase separation and structural order.
This study demonstrates that while AlphaFold-predicted GLUT4 models fail to capture the necessary conformational plasticity and hydration dynamics for accurate thermodynamic profiling of glucose translocation, native Cryo-EM structures reveal a functional Proline hinge mechanism essential for allosteric gating that is disrupted in rigid AI-generated architectures.
This study reveals that high-sensitivity FT-IR spectroscopy detects significant secondary structural divergence in photoactive yellow protein family members and their resurrected ancestors that AlphaFold failed to predict, highlighting a critical limitation of the AI model in capturing evolutionary structural changes despite high sequence similarity.
This study combines multi-microsecond molecular dynamics simulations and cryo-electron microscopy to reveal that prestin's electromechanical transduction involves conformational changes and anion-binding mechanisms that closely parallel the transport cycle of the related SLC26 family member pendrin, despite differences in ion accessibility and transition speeds.
This study demonstrates that a blind, three-gate hierarchical Gompertz procedure can detect early multiphase aggregation in human IL-1ra turbidity traces at protein concentrations as low as 5 mg/mL, revealing distinct kinetic events prior to the introduction of any rate or aggregate-mass data.