Biophysical journal最新文献_第4页

Computational modeling of microstreaming-induced disruption of Staphylococcus aureus biofilms 微流诱导的金黄色葡萄球菌生物膜破坏的计算模型

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-29 DOI: 10.1016/j.bpj.2026.09.035

Hongchen Li,Safae Oukrich,Kirby R. Lattwein,Nico de Jong,Martin D. Verweij,Kartik Jain,Klazina Kooiman

{"title":"Computational modeling of microstreaming-induced disruption of Staphylococcus aureus biofilms","authors":"Hongchen Li,Safae Oukrich,Kirby R. Lattwein,Nico de Jong,Martin D. Verweij,Kartik Jain,Klazina Kooiman","doi":"10.1016/j.bpj.2026.09.035","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.035","url":null,"abstract":"Staphylococcus aureus presents significant challenges in clinical settings due to its ability to form resilient biofilms, which drive persistent infections on medical implants and at wound sites. These bacteria are the leading cause of biomaterial-associated infections, often leading to implant failure. Moreover, S. aureus can form biofilms on cardiovascular implants, further complicating device-related infections. Cavitation microstreaming, generated by ultrasound-activated microbubbles through their oscillations, has emerged as a promising method for disrupting biofilms. However, the underlying biofilm-microstreaming interactions governing bacterial detachment remain poorly understood. In this study, a computational framework integrating coarse-grained molecular dynamics with the lattice Boltzmann method was developed to simulate Staphylococcus aureus biofilm growth and its response to microstreaming. The modeled biofilm morphology closely aligns with experimental confocal microscopy data, with less than 14% deviation in spatial spreading and roughness. To assess biofilm disruption, we applied microstreaming fields with dipole and quadrupole flow patterns at representative speeds of 1, 5, and 10 mm/s. Our results demonstrate that higher flow velocities facilitate greater detachment, with dipole flows inducing gradual erosion and quadrupole flows causing more localized disruption. By integrating computational modeling with experimental validation, this work provides a robust platform to investigate and maximize biofilm–microstreaming interactions. These findings emphasize the potential of ultrasound-activated microbubble-induced microstreaming as a noninvasive strategy for biofilm removal and provide a foundation for future therapeutic approaches.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"76 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149070979","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Artificial DNA-nano/microparticle motors: Factors governing speed, run length, and unidirectionality revealed by geometry-based kinetic simulations 人造dna -纳米/微粒马达：由几何动力学模拟揭示的控制速度、运行长度和单向性的因素

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-29 DOI: 10.1016/j.bpj.2026.09.041

Takanori Harashima,Ryota Iino

{"title":"Artificial DNA-nano/microparticle motors: Factors governing speed, run length, and unidirectionality revealed by geometry-based kinetic simulations","authors":"Takanori Harashima,Ryota Iino","doi":"10.1016/j.bpj.2026.09.041","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.041","url":null,"abstract":"DNA-nano/microparticle motors are burnt-bridge Brownian ratchets (BBR) moving on an RNA-modified two-dimensional surface driven by Ribonuclease H (RNase H), and are one of the fastest artificial molecular motors. Interestingly, these motors with moderate GC contents show processive rolling motion with a characteristic speed of ∼30 nm s−1 irrespective of particle size ranging from 100 to 5000 nm, whereas run length increases with particle size. Here we performed geometry-based kinetic simulations of DNA-nano/microparticle motors with the sizes of 100, 500, 1000, and 5000 nm to identify factors governing speed, run length, and unidirectionality. The simulations reproduced experimental trends: run length and unidirectionality increased with particle size, whereas median speed varied within a relatively narrow range of 20–50 nm s−1. This weak particle-size dependence of speed was caused by a trade-off between step size and pause length, both of which increased with particle size. In contrast, the run length and the unidirectionality increased with the particle size because large particles had high multivalency which suppresses stochastic detachment of the motor, high RNA hydrolysis efficiency under the motor trajectory which realizes almost perfect BBR motion, and stepping direction highly biased to forward. For all particle sizes examined, the speed increased from ∼20–30 to ∼220–250 nm s−1 by 10-fold increases in DNA/RNA hybridization, RNase H binding, and RNA hydrolysis rates (from 0.8 to 8.0, 7.2 to 72, and 3.0 to 30 s−1, respectively), even when considering the rotational diffusion of these particles. However, for the largest 5000-nm motor, the duration of rotational diffusion (∼0.04 s) reached ∼13% of the pause length (∼0.30 s) under the fast kinetic condition, decreasing the median speed from 250 to 220 nm s−1. Our results indicate that small DNA-particle motors have a potential for further acceleration because the contribution of rotational diffusion remains small.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"111 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149070984","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A small processivity of kinesin-14 motors can enhance sliding velocity of antiparallel microtubules 减小kinesin-14电机的加工速度可以提高反平行微管的滑动速度

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-29 DOI: 10.1016/j.bpj.2026.09.040

Jie Wang,Yu-Ru Liu,Peng-Ye Wang,Ping Xie

{"title":"A small processivity of kinesin-14 motors can enhance sliding velocity of antiparallel microtubules","authors":"Jie Wang,Yu-Ru Liu,Peng-Ye Wang,Ping Xie","doi":"10.1016/j.bpj.2026.09.040","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.040","url":null,"abstract":"Members of kinesin-14 family motors, which can move toward the microtubule (MT) minus end, play roles in spindle assembly and maintenance during mitosis and meiosis. Some kinesin-14 motors are non-processive while others are processive. Here, we study both theoretically and numerically the dynamics of the MT gliding and relative sliding of antiparallel MTs by multiple kinesin-14 motors. We show that while the published experimental data on the MT gliding and sliding by multiple kinesin-14 HSET motors cannot be explained by considering that the HSET is non-processive, they are well explained by a model in which HSET has a small processivity. More interestingly, we find that an optimal small processivity of the kinesin-14 motor is present, under which the MT sliding by the multiple motors can attain maximal velocity. Moreover, we show that the non-processive motors have an evidently larger ability to accumulate at the minus ends of parallel MTs than the processive motors of even a very small processivity. These imply that while the kinesin-14 motors of the small processivity are more likely to function as maintaining antiparallel MTs in spindles, the non-processive motors are more likely to function as anchoring nearly parallel MTs at their minus ends to form spindle poles.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"151 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149070989","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

On the effect of applied lateral tension on the deformation energetics of biological membranes and the lipid dynamics within 施加侧向张力对生物膜变形能量学和膜内脂质动力学的影响

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-29 DOI: 10.1016/j.bpj.2026.09.038

Yein Christina Park,Giacomo Fiorin,José D. Faraldo-Gómez

{"title":"On the effect of applied lateral tension on the deformation energetics of biological membranes and the lipid dynamics within","authors":"Yein Christina Park,Giacomo Fiorin,José D. Faraldo-Gómez","doi":"10.1016/j.bpj.2026.09.038","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.038","url":null,"abstract":"A broad range of cellular functions involve transient or persistent changes in the morphology of lipid membranes, from the organellar to the molecular scale. By and large, the thermodynamics of protein-mediated remodeling, which often distort the membrane beyond its thermally accessible undulations, remain to be understood. Molecular Dynamics simulations enhanced by advanced sampling methods are uniquely suited to examine and quantitate these phenomena. Here, we leverage the Multi-Map simulation method to directly quantify how applied lateral tension impacts the energetics of both global and localized membrane perturbations induced extrinsically. We obtain free-energy profiles of curvature and thickness deformations with and without tension, which allow us to test the quadratic approximations of Helfrich-based continuum theories. We find that these continuum models are applicable up to ∼ 20 kBT, beyond which they under-estimate the free-energy cost of bending. However, we find that the effect of tension on these deformations is primarily driven by changes in the projected area of the membrane, and therefore consistent with continuum theory, even beyond 30 kBT. These changes outpace the effects of tension on lipid packing and diffusion, and importantly we find that tension levels preceding rupture (≤ 10 mN/m) do not impede complete lipid mixing. Finally, we investigate the free-energy landscapes of membrane thickness and lipid enrichment with a heterogeneous lipid composition and show that strong enrichment can be sustained even under steady exchange of the constituent lipid molecules.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"222 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149070980","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Ground-state chromophore geometry, not cage size, tracks quantum yield in fluorescent proteins 基态发色团几何形状，而不是笼大小，跟踪荧光蛋白的量子产率

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-29 DOI: 10.1016/j.bpj.2026.09.042

Marc Zimmer

{"title":"Ground-state chromophore geometry, not cage size, tracks quantum yield in fluorescent proteins","authors":"Marc Zimmer","doi":"10.1016/j.bpj.2026.09.042","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.042","url":null,"abstract":"A common explanation for brightness variation in fluorescent proteins (FPs) is that tight chromophore cages produce bright proteins. This model predicts that quantum yield should track the dihedral rotational space available to the chromophore. We tested that prediction across 838 FP crystal structures from the Protein Data Bank.\u0000For each structure, we scanned the chromophore's two methine-bridge torsions, τ and φ. We measured two features of the chromophore environment: the fraction of torsional space that is sterically accessible, and the angular distance from the deposited chromophore to the nearest planar geometry. The scan shows a consistent family-wide asymmetry. The I-bond, the cis-trans isomerization axis, is clamped in all color classes. The P-bond, the ring-rotation axis, is the variable degree of freedom. Gatekeeper analysis identifies position 203, in avGFP numbering, as the dominant P-bond constraint. It is the first steric barrier in 21% of all sweep events.\u0000Cage size does not generally track quantum yield; instead, it primarily reflects chromophore chemistry. Indole-based cyan FPs and acylimine-based red FPs have the tightest cages, while imidazole-based blue FPs have the loosest. In red FPs, quantum yield is associated instead with ground-state chromophore geometry. More twisted crystallographic chromophores are consistently dimmer in red FPs.\u0000The scan also shows that rigidity is not a single property. Cage size, ground-state geometry, gatekeeper residues, and thermal immobilization are distinct measures of rigidity, each with a different relationship to quantum yield. Fluorescent-protein design should therefore target local control of chromophore geometry rather than global cage tightening.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"63 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149070985","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Enthalpy–Entropy Compensation in Inhibitor Binding to Carbonic Anhydrase Isozymes 抑制剂与碳酸酐酶同工酶结合的焓熵补偿

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-27 DOI: 10.1016/j.bpj.2026.09.032

Vaida Paketurytė-Latvė,Audrius Zakšauskas,Visvaldas Kairys,Edita Čapkauskaitė,Martynas Bagdonas,Alexey Smirnov,Elena Manakova,Saulius Gražulis,Daumantas Matulis

{"title":"Enthalpy–Entropy Compensation in Inhibitor Binding to Carbonic Anhydrase Isozymes","authors":"Vaida Paketurytė-Latvė,Audrius Zakšauskas,Visvaldas Kairys,Edita Čapkauskaitė,Martynas Bagdonas,Alexey Smirnov,Elena Manakova,Saulius Gražulis,Daumantas Matulis","doi":"10.1016/j.bpj.2026.09.032","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.032","url":null,"abstract":"Enthalpy–entropy compensation is a widely observed feature of protein–ligand recognition, yet its structural origins remain difficult to resolve. Here, we investigate a matched series of sulfonamide inhibitors binding to three closely related human carbonic anhydrase isozymes (CA II, CA XII, and CA XIII) using isothermal titration calorimetry, fluorescence thermal shift assays, and high-resolution X-ray crystallography. Although these isozymes share nearly identical overall folds and exhibit highly similar intrinsic Gibbs energies of binding, their enthalpic and entropic contributions diverge markedly. Correction of all observed thermodynamic quantities for proton-linked equilibria reveals that this divergence originates from subtle differences in the active-site microenvironment. In particular, single-residue variations—including the Thr/Thr/Val substitution at position 200, the Phe/Ala/Phe variation at position 131, and the Asn/Asn/Ser difference at position 62—modulate hydrogen-bond geometry, steric complementarity, and local solvation, thereby reshaping the balance between enthalpic and entropic driving forces. These results demonstrate how closely related proteins can achieve similar binding affinities through distinct energetic strategies and establish a coherent structure–thermodynamics framework for sulfonamide recognition.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"33 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149067321","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Nanoscale spatial confinement of proton flux by cardiolipin drives high-speed lateral proton transport in mitochondria 心磷脂对质子通量的纳米尺度空间限制驱动线粒体中质子的高速横向运输

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-26 DOI: 10.1016/j.bpj.2026.09.037

Ismail Adeniran,Hans Degens

{"title":"Nanoscale spatial confinement of proton flux by cardiolipin drives high-speed lateral proton transport in mitochondria","authors":"Ismail Adeniran,Hans Degens","doi":"10.1016/j.bpj.2026.09.037","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.037","url":null,"abstract":"Cellular respiration depends on the rapid, lateral flow of protons along the inner mitochondrial membrane to drive ATP synthesis. The precise nanoscale thermodynamic forces confining protons to this “local circuit” remain highly debated. Previous attempts to model macroscopic interfacial proton diffusion have been hindered by parameter equifinality and geometric artifacts, preventing the deconvolution of structural water networks from lipid electrostatics. Here, we address this ambiguity using a constrained, high-resolution two-dimensional continuum model. By incorporating experimentally validated buffer proton consumption rates as strict biological priors, we break mathematical degeneracy and isolate the specific effective spatial components of planar lipid bilayers. Calibrating our model against time-resolved DOPG fluorescence kinetics, we decouple a universal structural water barrier (5.7kBT) from the specific -1e electrostatic trap (4.3kBT). Extrapolating these first principles, we predict the confinement architecture of cardiolipin, the signature -2e dimeric lipid of mitochondria. Our simulations reveal a deep 14.3kBT phenomenological potential well. Crucially, this massive barrier confines protons within 1 to 2 nanometres of the membrane surface, virtually abolishing vertical leakage into the bulk aqueous phase of the inter-membrane space. Our simulations suggest that this spatial confinement triggers “dimensional squeezing”, preserving a robust lateral concentration gradient that actively accelerates radial proton wave propagation. Biologically, these findings reveal that cardiolipin does not merely prevent proton dissipation, we predict it functions as a highly efficient, quasi-two-dimensional nanoscale antenna that captures and rapidly channels protons directly to ATP synthase, ensuring the kinetic viability of eukaryotic energy production.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"17 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149050313","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Role of ligand-dependent conformational modulation of TNPO3 HEAT-repeat solenoid in nuclear import 配体依赖的TNPO3热重复螺线管构象调制在核进口中的作用

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-26 DOI: 10.1016/j.bpj.2026.09.036

Sonali Chatterjee,Atanu Maity,Ranjit Prasad Bahadur

{"title":"Role of ligand-dependent conformational modulation of TNPO3 HEAT-repeat solenoid in nuclear import","authors":"Sonali Chatterjee,Atanu Maity,Ranjit Prasad Bahadur","doi":"10.1016/j.bpj.2026.09.036","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.036","url":null,"abstract":"Transportin-3 (TNPO3) is a HEAT-repeat nuclear transport receptor that mediates nuclear import of serine/arginine-rich (SR) proteins and interacts with Ran GTPase during nuclear transport cycle. Although structures of several TNPO3 complexes are available, how ligand binding modulates the conformational landscape of the receptor remains poorly understood. Here, we combine microsecond-scale molecular dynamics simulations with umbrella sampling free-energy calculations to investigate how SR cargo binding, Ran nucleotide state and cargo phosphorylation regulate TNPO3 conformational dynamics. Equilibrium simulations show that apo TNPO3 samples a broad conformational ensemble, while ligand binding substantially reshapes the conformational landscape. SR cargo protein stabilizes a partially extended solenoid architecture and introduces an energetic penalty to prevent further opening. Ran binding favours compact conformations of TNPO3 scaffold. Among these states, Ran-GTP produces the strongest confined conformational ensemble, while Ran-GDP allows broader structural variability. State-resolved structural analysis indicates that these energetic differences arise from ligand-dependent modulation of interface packing and hydrogen-bond networks. The modulation propagates across the HEAT-repeat array and alters global solenoid curvature. Reduction in phosphorylation of SR cargo weakens binding and increases conformational heterogeneity, highlighting the role of phosphorylation in stabilizing the TNPO3-cargo interface. These findings support a ligand-dependent conformational pathway, in which TNPO3 shifts from a flexible apo ensemble to an SR-bound extended state. This is followed by a structurally compatible intermediate shared with Ran-GTP-bound form before reaching compact Ran-GTP-stabilized state associated with cargo release. Together, these results provide a quantitative framework for understanding how ligand binding reshapes TNPO3 conformations during nuclear transport cycle.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"63 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149050294","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Probing the native state of a two-state folding protein by high pressure NMR spectroscopy 用高压核磁共振光谱法探测两态折叠蛋白的天然状态

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-23 DOI: 10.1016/j.bpj.2026.09.030

Frederic Berner,Michael Kovermann

{"title":"Probing the native state of a two-state folding protein by high pressure NMR spectroscopy","authors":"Frederic Berner,Michael Kovermann","doi":"10.1016/j.bpj.2026.09.030","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.09.030","url":null,"abstract":"The investigation of structural, dynamic and functional properties of proteins as a function of hydrostatic pressure can provide profound insights into e.g. protein folding or protein structure-function relationships. Precise structural information is required to elucidate the response a protein exhibits upon increasing hydrostatic pressure. High pressure (HP) NMR spectroscopy represents a powerful experimental approach to obtain such structural information at atomic resolution. Here, we exploit the distance dependence of the nuclear Overhauser effect (NOE) to determine intramolecular 1H – 1H distances as a function of hydrostatic pressure for the cold shock protein B from Bacillus subtilis (BsCspB), a model protein undergoing a two-state folding-to-unfolding transition within the range applicable with HP NMR spectroscopy. Two independent approaches have been pursued in this study to determine intramolecular distances: (i) Making use of a reference NOE and (ii) Analyzing NOE build-up curves. Both approaches yield the same result: Intramolecular distances existing between the sheets that define the β-barrel fold of BsCspB have been shown to respond nonuniformly to increasing hydrostatic pressure. In fact, intramolecular distances increase, decrease or remain unchanged when hydrostatic pressure elevates. The majority of impacted sheet-to-sheet distances analyzed in the present study increase upon increasing hydrostatic pressure suggesting that the three-dimensional structure of native BsCspB is modified such that β-strands depart from each other. This ‘opening‘ possibly facilitates the penetration of solvent molecules into the interior of BsCspB and may represent an initial step for the pressure-induced folding-to-unfolding transition.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"88 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149019670","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Estimating the Kinetic Prefactor for Membrane Tube Fission from Fluctuation Dynamics 从波动动力学估计膜管裂变的动力学前因子

IF 3.4 3区生物学

Biophysical journal Pub Date : 2026-09-23 DOI: 10.1016/j.bpj.2026.09.027

Russell Spencer,Alireza Soleimani,Marcus Müller

引用次数: 0