329 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.
The adhesion of spherical nanoparticles to membranes promotes the formation of energetically favorable membrane tubules through cooperative wrapping, which minimizes total energy by creating two contact regions per particle compared to the single region in individual wrapping, with the resulting energy gain depending significantly on the adhesion potential range and membrane tension.
This paper presents a high-performance, computer-controlled bipedal DNA motor that utilizes a fuel-before-antifuel scheme and automated microfluidics to achieve programmable, bidirectional motion with >98% step yield and efficiencies up to four orders of magnitude higher than previous externally controlled DNA walkers.
This paper introduces ATLAS, a comprehensive 3D RNA motif library that utilizes graph representations to incorporate non-Watson-Crick interactions and pseudoknots, enabling advanced motif-based structure prediction, design, and evolutionary analysis through a novel similarity metric and physics-inspired model.
This paper presents an enzyme-free, fuel-driven DNA system that overcomes product inhibition to achieve catalytic molecular templating, enabling sequence-specific information propagation and controlled assembly of copolymer products.
This study utilizes microsecond constant-pH molecular dynamics simulations to demonstrate that the membrane environment, specifically lipid composition and phase behavior, significantly lowers the pKa of ionizable lipids and drives distinct pH-dependent structural rearrangements, thereby providing quantitative design principles for optimizing lipid nanoparticle delivery performance.
This study demonstrates that the non-monotonic magnetic field-dependent fluorescence observed in *E. coli* expressing the engineered flavoprotein MagLOV2 is consistent with the radical pair mechanism, characterized by a positive effect peaking near 1 mT, a sign reversal at 2 mT, and saturation above 70 mT.
This study demonstrates that ratiometric signaling, where G proteins integrate information from both bound and unbound receptors to create an unbiased, time-averaged signal, enables cells to overcome noise from low receptor numbers and surpass theoretical limits for accurate gradient sensing.
This paper introduces HXMS, a standardized, lightweight file format that preserves full isotopic mass spectra and comprehensive experimental metadata for Hydrogen/Deuterium Exchange-Mass Spectrometry (HX-MS) data, along with PFLink, a Python tool to convert existing software outputs into this format to enable more quantitative analysis, better data sharing, and future machine learning applications.
Cryo-EM structures and biochemical analyses reveal that *Paracoccus* TMAO demethylase functions as a bifunctional enzyme that channels unstable formaldehyde intermediates from its catalytic core to a remote tetrahydrofolate-binding site, thereby coupling TMAO degradation with one-carbon metabolism to enhance efficiency and prevent toxicity.
This study utilizes in-cell cryo-electron tomography to demonstrate that type I kinase inhibitors (MLi-2) promote extensive microtubule-associated LRRK2 filament formation and bundling, enabling the construction of a full-length structural model, whereas type II inhibitors (GZD-824) prevent such assemblies.