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 presents a computational framework that successfully simulates the hemodynamic changes in pulmonary wave intensity and flow redistribution following lung resection by modeling arterial network alterations, with results showing strong agreement with clinical data and validating the model's potential for future patient-specific applications.
This study reveals that the intrinsically disordered region (IDR) of the transcription factor ComK, rather than the protein binding itself, amplifies long-range DNA fluctuations to enable allostery, whereas its removal rigidifies the DNA and abolishes transcriptional function.
This study demonstrates that in living human cells, transcriptional specificity is achieved through an energy-dependent kinetic proofreading mechanism where promoters act as dwell-time detectors, allowing the glucocorticoid receptor to discriminate between specific and non-specific binding sites via ATP-driven processes like neddylation and chromatin remodeling.
This study utilizes large-scale molecular dynamics simulations to demonstrate that GAG helical conformations are driven by L-iduronic acid stabilization via specific sulfation patterns and introduces a quantitative two-parameter metric to objectively classify these secondary structures.
Using multi-color single-molecule fluorescence microscopy, this study reveals that the stable, minutes-long assembly of the rrnTAC complex, driven by SuhB recruitment, is essential for reducing RNAP pausing and enhancing co-transcriptional rRNA processing, distinguishing the functional dynamics of rRNA transcription from the transient interactions typical of mRNA transcription.
This paper introduces a computationally efficient workflow that utilizes Mean-Shift Super-Resolution (MSSR) to generate intensity-based spatial masks, effectively mitigating PSF-driven spatio-temporal signal mixing in Fluorescence Lifetime Imaging Microscopy (FLIM) and restoring accurate lifetime signatures without altering the underlying temporal decay kinetics.
This study presents high-resolution cryo-EM structures of native *E. coli* efflux complexes that reveal the previously uncharacterized lipoprotein YbjP acts as a crucial structural component anchoring TolC to the outer membrane and accommodating conformational changes during the complete drug transport cycle.
This study presents a predictive mechanochemical modeling framework that simulates how nuclear deformation induced by nanopillar substrates influences lamin remodeling and nucleocytoplasmic transport, revealing that specific nanotopographies maximize envelope tension and that lamin depletion significantly increases rupture risk, a finding subsequently validated experimentally.
Using high-speed atomic force microscopy, this study reveals the real-time mechanism by which G2L4 reverse transcriptase dimers facilitate microhomology-mediated end joining through DNA binding, gap filling, and terminal transferase activity, while T4 DNA ligase stabilizes the repaired products by sealing nicks and suppressing off-pathway branching.
This study reveals that ATP synthase possesses an intrinsic electrostatic potential that directly modulates the local proton-motive force experienced by its motor, acting as a species-specific modifier of oxidative phosphorylation efficiency that can either enhance or reduce ATP yield depending on the enzyme's structural polarity.