Pub Date : 2026-01-20Epub Date: 2025-07-07DOI: 10.1016/j.bpj.2025.07.001
Arriën Symon Rauh, Gustav Stausbøll Hedemark, Giulio Tesei, Kresten Lindorff-Larsen
Protein phosphorylation is a common and essential post-translational modification that affects biochemical properties and regulates biological activities. Phosphorylation is particularly common for intrinsically disordered proteins and can significantly modulate their function and potential to interact with binding partners. To understand the biophysical origins of how phosphorylation of disordered proteins influences their function, it is valuable to investigate how the modifications lead to changes in their conformational ensembles. Here, we have used a top-down data-driven approach to develop a coarse-grained molecular dynamics model compatible with the CALVADOS protein simulation model to study the effects of serine and threonine phosphorylation on the global structural properties of disordered proteins. We parameterize the model using experimental data on the effects of phosphorylation on global dimensions. By comparing with baseline models and simulations using the phosphomimetics aspartate and glutamate, we show that the effect of phosphorylation on the global dimensions of disordered proteins is mostly driven by the additional charge. We envisage that our model can be applied to study the effects of phosphorylation of disordered proteins at the proteome scale as well as to study the important roles of protein phosphorylation on phase separation.
{"title":"A coarse-grained model for simulations of phosphorylated disordered proteins.","authors":"Arriën Symon Rauh, Gustav Stausbøll Hedemark, Giulio Tesei, Kresten Lindorff-Larsen","doi":"10.1016/j.bpj.2025.07.001","DOIUrl":"10.1016/j.bpj.2025.07.001","url":null,"abstract":"<p><p>Protein phosphorylation is a common and essential post-translational modification that affects biochemical properties and regulates biological activities. Phosphorylation is particularly common for intrinsically disordered proteins and can significantly modulate their function and potential to interact with binding partners. To understand the biophysical origins of how phosphorylation of disordered proteins influences their function, it is valuable to investigate how the modifications lead to changes in their conformational ensembles. Here, we have used a top-down data-driven approach to develop a coarse-grained molecular dynamics model compatible with the CALVADOS protein simulation model to study the effects of serine and threonine phosphorylation on the global structural properties of disordered proteins. We parameterize the model using experimental data on the effects of phosphorylation on global dimensions. By comparing with baseline models and simulations using the phosphomimetics aspartate and glutamate, we show that the effect of phosphorylation on the global dimensions of disordered proteins is mostly driven by the additional charge. We envisage that our model can be applied to study the effects of phosphorylation of disordered proteins at the proteome scale as well as to study the important roles of protein phosphorylation on phase separation.</p>","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":" ","pages":"396-405"},"PeriodicalIF":3.1,"publicationDate":"2026-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144590373","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}
Pub Date : 2026-01-19DOI: 10.1016/j.bpj.2026.01.024
Pauline Delpierre, Marc Lefranc
{"title":"A minimal activator-inhibitor-repressor model of the hepatic circadian clock","authors":"Pauline Delpierre, Marc Lefranc","doi":"10.1016/j.bpj.2026.01.024","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.01.024","url":null,"abstract":"","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"115 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146000871","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}
Pub Date : 2026-01-16DOI: 10.1016/j.bpj.2026.01.026
Matthias Häring,Yuanshu Zhang,Na Zhang,Edward S Allgeyer,Jennifer H Richens,George Sirinakis,Zhiyi Lv,Daniel St Johnston,Fred Wolf,Jörg Großhans,Deqing Kong
Cell junction remodeling is central to epithelial morphogenesis and tissue rheology, and depends on the interplay between adhesion molecules and the actomyosin cortex. E-cadherin constitutes the molecular basis for epithelial cell adhesion, while cortical actomyosin plays a major role in intracellular force generation. However, the precise nanoscale organization and relationship between F-actin and E-cadherin at the cell interface still remain insufficiently understood. Here, we applied super-resolution DNA/peptide-PAINT microscopy to reveal the nanoscopic clustering of E-cadherin and its junctional distribution in relation to cortical F-actin at adherens junctions in the Drosophila embryonic epidermis. We were able to resolve distinct pairs of E-cadherin clusters approximately 45 nm apart on opposite sides of the adherens junctions. Intriguingly, these paired clusters were interspersed with unpaired clusters, lacking corresponding counterparts across the junction. We observed that cluster size, spatial arrangement, and cross-junction matching change during development and depend on N-glycosylation, a post-translational modification affecting E-cadherin. Moreover, the organization of F-actin cortices between neighboring cells were found to be strongly correlated at junctions. Contrary to expectations, this intercellular F-actin correlation was observed independently of E-cadherin. Our study provides new insights into the nanoscale organization of adherens junctions, opening a window into the molecular mechanism of adhesion and mechanics of epithelial cells during morphogenesis.
{"title":"DNA-PAINT resolves E-cadherin-independent cross-junctional F-actin organization in Drosophila embryonic tissue.","authors":"Matthias Häring,Yuanshu Zhang,Na Zhang,Edward S Allgeyer,Jennifer H Richens,George Sirinakis,Zhiyi Lv,Daniel St Johnston,Fred Wolf,Jörg Großhans,Deqing Kong","doi":"10.1016/j.bpj.2026.01.026","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.01.026","url":null,"abstract":"Cell junction remodeling is central to epithelial morphogenesis and tissue rheology, and depends on the interplay between adhesion molecules and the actomyosin cortex. E-cadherin constitutes the molecular basis for epithelial cell adhesion, while cortical actomyosin plays a major role in intracellular force generation. However, the precise nanoscale organization and relationship between F-actin and E-cadherin at the cell interface still remain insufficiently understood. Here, we applied super-resolution DNA/peptide-PAINT microscopy to reveal the nanoscopic clustering of E-cadherin and its junctional distribution in relation to cortical F-actin at adherens junctions in the Drosophila embryonic epidermis. We were able to resolve distinct pairs of E-cadherin clusters approximately 45 nm apart on opposite sides of the adherens junctions. Intriguingly, these paired clusters were interspersed with unpaired clusters, lacking corresponding counterparts across the junction. We observed that cluster size, spatial arrangement, and cross-junction matching change during development and depend on N-glycosylation, a post-translational modification affecting E-cadherin. Moreover, the organization of F-actin cortices between neighboring cells were found to be strongly correlated at junctions. Contrary to expectations, this intercellular F-actin correlation was observed independently of E-cadherin. Our study provides new insights into the nanoscale organization of adherens junctions, opening a window into the molecular mechanism of adhesion and mechanics of epithelial cells during morphogenesis.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"390 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145993055","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}
Pub Date : 2026-01-16DOI: 10.1016/j.bpj.2026.01.016
Prasheel Nakate,Arezoo M Ardekani
Lipid nanoparticles (LNPs) traverse through multiple biological barriers, such as crosslinked mesh structures in the extracellular matrix, before reaching their target sites. The physicochemical properties of LNPs determine their ability to penetrate complex biological environments such as the brain extracellular matrix. Their deformation in polymeric matrices affects transport, making it crucial to understand these factors for effective therapeutic delivery. Here, we develop a highly Coarse-Grained (CG) model of the LNP and its surrounding polymeric matrix, simulated as a uniform grid of cross-linked hyaluronic acid (HA) chains. The model for highly coarse-grained LNP was developed from a one-particle-thick membrane model that maintains mechanical features of lipid membranes, such as fluidity, topological changes, and hydrodynamic effects. Here, we investigate the collective influence of lipid nanoparticle size and its bending rigidity on the diffusive transport through the biological matrix. Our work highlights the role of particle to matrix size ratio in understanding deformation assisted diffusive transport of LNPs in the matrix environment. Our study provides a tool to disentangle the effects of particle size and their bending rigidity on the transport through complex environments. Furthermore, this study systematically complements the rational design of lipid nanoparticle-based drug delivery platforms.
{"title":"Modeling lipid nanoparticle transport in extracellular matrix: Effects of particle size and rigidity.","authors":"Prasheel Nakate,Arezoo M Ardekani","doi":"10.1016/j.bpj.2026.01.016","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.01.016","url":null,"abstract":"Lipid nanoparticles (LNPs) traverse through multiple biological barriers, such as crosslinked mesh structures in the extracellular matrix, before reaching their target sites. The physicochemical properties of LNPs determine their ability to penetrate complex biological environments such as the brain extracellular matrix. Their deformation in polymeric matrices affects transport, making it crucial to understand these factors for effective therapeutic delivery. Here, we develop a highly Coarse-Grained (CG) model of the LNP and its surrounding polymeric matrix, simulated as a uniform grid of cross-linked hyaluronic acid (HA) chains. The model for highly coarse-grained LNP was developed from a one-particle-thick membrane model that maintains mechanical features of lipid membranes, such as fluidity, topological changes, and hydrodynamic effects. Here, we investigate the collective influence of lipid nanoparticle size and its bending rigidity on the diffusive transport through the biological matrix. Our work highlights the role of particle to matrix size ratio in understanding deformation assisted diffusive transport of LNPs in the matrix environment. Our study provides a tool to disentangle the effects of particle size and their bending rigidity on the transport through complex environments. Furthermore, this study systematically complements the rational design of lipid nanoparticle-based drug delivery platforms.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"40 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145993065","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}
Pub Date : 2026-01-15DOI: 10.1016/j.bpj.2026.01.022
Camille Rodriguez, Hyuntae Jeong, Jiwon Kim, Lily A Cordner, Paul Cao, Suganya Sivagurunathan, Stephen A Adam, Robert D Goldman, Ian Y Wong, Ming Guo
During a variety of physiological and pathological processes, such as development, wound healing, and tumor progression, epithelial cells collectively invade into their surroundings. Vimentin intermediate filaments (VIFs) are often observed to play a role in the epithelial cells located at the margins of 2D cultures. However, their role in 3D collective cell behavior remains underexplored. Here, we investigate how induced vimentin expression affects 3D multicellular architecture and mechanics in luminal breast cancer cells (MCF-7) that ordinarily express keratin intermediate filaments only. We find that vimentin expression significantly alters 3D cell cluster morphology, inducing protrusions and increasing boundary fluctuations. Furthermore, cells in vimentin-expressing clusters show enhanced, more stochastic migration. In addition, these clusters exert stronger and localized traction forces on the surrounding matrix, indicating increased cell-matrix interactions. Transcriptomic analysis corroborates these biophysical findings, revealing upregulated gene expression for cell migration and matrix adhesion and downregulated cell-cell adhesion genes. Our results demonstrate that VIFs are critical in modulating 3D multicellular collective morphology and dynamics, promoting invasive-like behavior by enhancing cell migration and cell-matrix interactions. These results provide fundamental insights into understanding tissue morphogenesis and disease progression.
{"title":"Expression of vimentin intermediate filaments in epithelial cells promotes cell migration and cell-matrix interaction in 3D.","authors":"Camille Rodriguez, Hyuntae Jeong, Jiwon Kim, Lily A Cordner, Paul Cao, Suganya Sivagurunathan, Stephen A Adam, Robert D Goldman, Ian Y Wong, Ming Guo","doi":"10.1016/j.bpj.2026.01.022","DOIUrl":"10.1016/j.bpj.2026.01.022","url":null,"abstract":"<p><p>During a variety of physiological and pathological processes, such as development, wound healing, and tumor progression, epithelial cells collectively invade into their surroundings. Vimentin intermediate filaments (VIFs) are often observed to play a role in the epithelial cells located at the margins of 2D cultures. However, their role in 3D collective cell behavior remains underexplored. Here, we investigate how induced vimentin expression affects 3D multicellular architecture and mechanics in luminal breast cancer cells (MCF-7) that ordinarily express keratin intermediate filaments only. We find that vimentin expression significantly alters 3D cell cluster morphology, inducing protrusions and increasing boundary fluctuations. Furthermore, cells in vimentin-expressing clusters show enhanced, more stochastic migration. In addition, these clusters exert stronger and localized traction forces on the surrounding matrix, indicating increased cell-matrix interactions. Transcriptomic analysis corroborates these biophysical findings, revealing upregulated gene expression for cell migration and matrix adhesion and downregulated cell-cell adhesion genes. Our results demonstrate that VIFs are critical in modulating 3D multicellular collective morphology and dynamics, promoting invasive-like behavior by enhancing cell migration and cell-matrix interactions. These results provide fundamental insights into understanding tissue morphogenesis and disease progression.</p>","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":" ","pages":""},"PeriodicalIF":3.1,"publicationDate":"2026-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145987932","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}
Pub Date : 2026-01-14DOI: 10.1016/j.bpj.2026.01.020
Saeed Ahmad,Debangana Mukhopadhyay,Rajdeep Grewal,Ciriyam Jayaprakash,Jayajit Das
Natural Killer (NK) cells are lymphocytes of the innate immunity and sense healthy or diseased target cells with activating and inhibitory NK cell receptor (NKR) molecules expressed on the cell surface. The protection provided by NK cells against viral infections and tumors critically depends on their ability to distinguish healthy cells from diseased target cells that express 100-fold more activating ligands. NK cell signaling and activation depend on integrating opposing signals initiated by activating and inhibitory NKRs interacting with the cognate ligands expressed on target cells. Imaging experiments show that both activating and inhibitory NKRs in the plasma membrane form submicron-sized clusters in resting NK cells. How do these submicron size NKR clusters formed in the resting state affect signal discrimination? Using in silico mechanistic signaling modeling combined with information theory and published super-resolution imaging data for two well-studied human NKRs, activating NKG2D and inhibitory KIR2DL1, we show that early time signal discrimination by NK cells depends on the spatial statistics of these clusters. Modeling shows when NKG2D and KIR2DL1 clusters are disjoint in the resting state, these clusters help NK cells to discriminate between target cells expressing low and high levels of the activating cognate ligand, whereas, when the NKR clusters show high degree of overlap it prevents NK cells from differentiating healthy from diseased target cells. Therefore, the spatial statistics of submicron scale clusters of activating and inhibitory NKRs at the resting state provides an additional layer of control for signal discrimination in NK cells.
{"title":"Resting-state spatial statistics of NK cell receptors may improve early signal discrimination.","authors":"Saeed Ahmad,Debangana Mukhopadhyay,Rajdeep Grewal,Ciriyam Jayaprakash,Jayajit Das","doi":"10.1016/j.bpj.2026.01.020","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.01.020","url":null,"abstract":"Natural Killer (NK) cells are lymphocytes of the innate immunity and sense healthy or diseased target cells with activating and inhibitory NK cell receptor (NKR) molecules expressed on the cell surface. The protection provided by NK cells against viral infections and tumors critically depends on their ability to distinguish healthy cells from diseased target cells that express 100-fold more activating ligands. NK cell signaling and activation depend on integrating opposing signals initiated by activating and inhibitory NKRs interacting with the cognate ligands expressed on target cells. Imaging experiments show that both activating and inhibitory NKRs in the plasma membrane form submicron-sized clusters in resting NK cells. How do these submicron size NKR clusters formed in the resting state affect signal discrimination? Using in silico mechanistic signaling modeling combined with information theory and published super-resolution imaging data for two well-studied human NKRs, activating NKG2D and inhibitory KIR2DL1, we show that early time signal discrimination by NK cells depends on the spatial statistics of these clusters. Modeling shows when NKG2D and KIR2DL1 clusters are disjoint in the resting state, these clusters help NK cells to discriminate between target cells expressing low and high levels of the activating cognate ligand, whereas, when the NKR clusters show high degree of overlap it prevents NK cells from differentiating healthy from diseased target cells. Therefore, the spatial statistics of submicron scale clusters of activating and inhibitory NKRs at the resting state provides an additional layer of control for signal discrimination in NK cells.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"62 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145986521","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}
Pub Date : 2026-01-14DOI: 10.1016/j.bpj.2026.01.017
Mandira Dutta, Gregory A. Voth
{"title":"Mutation and ACE2-induced Allosteric Network Rewiring in Delta and Omicron SARS-CoV-2 Spike Proteins","authors":"Mandira Dutta, Gregory A. Voth","doi":"10.1016/j.bpj.2026.01.017","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.01.017","url":null,"abstract":"","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"38 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145962555","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}
Pub Date : 2026-01-14DOI: 10.1016/j.bpj.2026.01.021
Luigi Catacuzzeno, Maurizio G. Cavaliere, Antonio Michelucci
{"title":"An approach based on Linear Programming to build experimentally-driven Pump-Leak models","authors":"Luigi Catacuzzeno, Maurizio G. Cavaliere, Antonio Michelucci","doi":"10.1016/j.bpj.2026.01.021","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.01.021","url":null,"abstract":"","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"39 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145962086","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}
Pub Date : 2026-01-14DOI: 10.1016/j.bpj.2026.01.025
Zachary T Bachler,Evelyn W Cheng,Maya N Arruda,C Swathi K Menon,Andrey V Struts,Alexander V Barmasov,Michael F Brown
Membranes possess characteristic lipidomes that are preserved by homeostatic regulation, even as environmental conditions change. Technological advancements in lipidomics instrumentation have revealed that altering this composition can produce significant physiological effects and can influence protein function. As lipidomics has expanded our view of membrane diversity, a key question remains: which membrane feature must be maintained by cells to ensure proper protein function? Here, we focus on key membrane properties-such as asymmetry, packing, and elasticity-and highlight cases in which lipid composition modulates protein function. We find that curvature stress is a likely target of such regulation and accounts for the gradual changes in protein activity observed across lipid series that differ systematically in their physical properties. Curvature stress arises when there is a difference between the actual (mean) and preferred (spontaneous) curvature of a membrane. The magnitude of the stress depends on the amount of deformation and the resistance of the membrane to bending (bending rigidity), both of which depend on lipid packing. These properties are further modulated by composition and number asymmetry between the two leaflets. Throughout these studies, rhodopsin has played a pivotal role in uncovering these principles due to its natural abundance and spectroscopic accessibility enabling experiments that would be difficult or impossible with other membrane proteins. We therefore consider rhodopsin as the hydrogen atom of membrane biophysics in recognition of its unparalleled significance as a model system, in analogy to how the hydrogen atom provided the foundation for atomic orbital theory. Because rhodopsin uniquely permits precise measurements of conformational equilibria, it remains a powerful system for dissecting how lipid composition and asymmetry give rise to membrane curvature adaptation.
{"title":"Rhodopsin: The Hydrogen Atom of Membrane Biophysics.","authors":"Zachary T Bachler,Evelyn W Cheng,Maya N Arruda,C Swathi K Menon,Andrey V Struts,Alexander V Barmasov,Michael F Brown","doi":"10.1016/j.bpj.2026.01.025","DOIUrl":"https://doi.org/10.1016/j.bpj.2026.01.025","url":null,"abstract":"Membranes possess characteristic lipidomes that are preserved by homeostatic regulation, even as environmental conditions change. Technological advancements in lipidomics instrumentation have revealed that altering this composition can produce significant physiological effects and can influence protein function. As lipidomics has expanded our view of membrane diversity, a key question remains: which membrane feature must be maintained by cells to ensure proper protein function? Here, we focus on key membrane properties-such as asymmetry, packing, and elasticity-and highlight cases in which lipid composition modulates protein function. We find that curvature stress is a likely target of such regulation and accounts for the gradual changes in protein activity observed across lipid series that differ systematically in their physical properties. Curvature stress arises when there is a difference between the actual (mean) and preferred (spontaneous) curvature of a membrane. The magnitude of the stress depends on the amount of deformation and the resistance of the membrane to bending (bending rigidity), both of which depend on lipid packing. These properties are further modulated by composition and number asymmetry between the two leaflets. Throughout these studies, rhodopsin has played a pivotal role in uncovering these principles due to its natural abundance and spectroscopic accessibility enabling experiments that would be difficult or impossible with other membrane proteins. We therefore consider rhodopsin as the hydrogen atom of membrane biophysics in recognition of its unparalleled significance as a model system, in analogy to how the hydrogen atom provided the foundation for atomic orbital theory. Because rhodopsin uniquely permits precise measurements of conformational equilibria, it remains a powerful system for dissecting how lipid composition and asymmetry give rise to membrane curvature adaptation.","PeriodicalId":8922,"journal":{"name":"Biophysical journal","volume":"83 1","pages":""},"PeriodicalIF":3.4,"publicationDate":"2026-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145986523","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}
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