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 targeted mutations at the subunit interface of the IGPS enzyme can rationally rewire its allosteric regulation by altering specific interfacial contacts, which reshapes the conformational ensemble and dynamic network to either constitutively activate or weaken effector-induced catalysis.
This study reveals that the assembly and nuclear organization of the FoxP1 transcription factor are governed by an antagonistic coupling between its leucine-zipper and Forkhead domains, where this multidomain balance regulates dimerization, DNA binding, and the formation of nuclear condensates, with disruptions leading to disease-associated dysregulation.
This study reveals that while collagen type II uniquely scaffolds full synovial fluid films whereas collagen type I does not, both collagen types similarly bind and retain recombinant lubricin, offering critical insights into the mechanical decline of osteoarthritic joints and the potential of lubricin-based therapies.
This study utilizes nanophotonic zero-mode waveguides to achieve single-molecule resolution of the sequential binding dynamics and intermediate conformational states of a cyclic nucleotide-gated ion channel in cell-derived vesicles, overcoming the concentration limitations of traditional diffraction-limited microscopy to reveal cooperative binding mechanisms.
By extending a kinetic Monte Carlo model to simulate how capsid assembly modulators (CAMs) preferentially bind to specific subunit interfaces, this study elucidates the thermodynamic and kinetic mechanisms by which these antivirals redirect Hepatitis B virus capsid assembly toward noninfectious, malformed structures, thereby advancing the development of HBV treatments and broader self-assembly strategies.
This study reveals that the translation initiation helicase eIF4A forms nanometer-scale RNA-protein clusters (RPCs) driven by the multivalent interactions of its cofactor eIF4B, a mechanism that is essential for coordinating ATP-dependent helicase activity and regulating translation initiation.
This study establishes a unified ensemble-allosteric framework demonstrating that pathogenic mutations in the IP3 receptor cause disease not by disrupting global protein structure, but by altering conformational ensemble probabilities and allosteric information flow to produce either gain- or loss-of-function phenotypes.
This study reveals that evolution has shaped mRNA sequences to minimize self-association and maintain transcriptome solubility, preventing the promiscuous RNA-RNA interactions that would otherwise cause widespread, non-functional clustering.
This paper demonstrates that continuously applying ultrasonic excitation during vitrification effectively overcomes preferred particle orientation in cryo-EM by mechanically disrupting protein adsorption at the air-water interface, offering a simple and widely applicable solution to a common imaging challenge.
This study demonstrates that assembling ordered aster structures from disordered microtubule and kinesin motor mixtures generates reproducible, long-lasting radial ATP and motor density gradients, revealing that maintaining these spatial motor gradients is the dominant energetic demand in such non-equilibrium cytoskeletal systems.