261 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.
Using a bespoke dripping-onto substrate rheometer, this study reveals that mucin solutions exhibit a concentration-dependent transition in extensional flow, shifting from linear thinning at low concentrations to elastocapillary thinning in semidilute regimes, before experiencing a sudden reduction in extensibility and relaxation time at higher concentrations due to inter-chain associations.
This paper presents a novel hybrid approach that validates AlphaFold2-predicted protein structures against NMR NOESY spectra using interresidue contact heuristics and a support vector machine, demonstrating its effectiveness in identifying inaccurate predictions and solving previously unsolved protein structures like LoTOP.
This study demonstrates that 2D Ti3C2Tx MXene nanosheets effectively capture Alzheimer's disease-specific plasma protein signatures by forming a distinct protein corona enriched with hnRNPs, annexins, and inflammatory mediators, thereby enabling robust molecular profiling and differentiation between patients and healthy controls.
This paper proposes a minimal model demonstrating that temperate phages can distinguish between lysis and lysogeny based on multiplicity of infection (MOI) only through specific coupling mechanisms, such as host enzymes, that create a fast-acting asymmetry between the two regulatory pathways.
This study presents the cryo-EM structure and biochemical characterization of a BRAF/CRAF heterodimer, revealing that while its overall organization resembles RAF homodimers, the negative charge in the N-terminal acidic (NtA) motif is not essential for activation, suggesting its role lies in modulating local backbone dynamics and conformational stability rather than specific interfacial recognition.
This study establishes a sustainable and reproducible framework for fabricating defined liposomal phases by optimizing hydration ratios, refining probe-sonication protocols to prevent overheating, and developing a Python-based machine-learning tool for vesicle size characterization.
This study utilized iPALM and PERPL analysis to map the high-precision 3D organization of ZASP, α-Actinin-2, and the Z1Z2 epitope of titin within cardiac muscle Z-discs, revealing that while ZASP and α-Actinin-2 share a similar repeating pattern, the Z1Z2 epitope exhibits a distinct structural arrangement.
This study reveals that Yoda molecules, previously thought to selectively activate PIEZO1, also effectively agonize PIEZO2 by increasing its open probability and slowing inactivation, with Yoda2's enhanced potency attributed to a specific salt bridge interaction, thereby necessitating a reevaluation of their use in distinguishing PIEZO channel functions.
This study develops a novel kinetic framework combining Lagrangian dynamics and Hill muscle equations to demonstrate that bipedal take-off mechanics scale efficiently across diverse body masses, confirming that *Tyrannosaurus rex* was capable of jumping while providing a new methodology for designing scalable bio-inspired robots.
The authors developed triplet tumbling microscopy (TTM), a versatile imaging technique that leverages infrared-triggerable triplet states to measure rotational diffusion in living cells, thereby enabling the real-time, in situ quantification of protein complex assembly, size, and dynamics without requiring prior knowledge of interacting partners.