Biological Sciences / Biophysics and Computational Biology -- New results matching your topic search. https://www.pnas.org/action/doSearch?af=R Proceedings of the National Academy of Sciences: Biophysics and Computational Biology Proceedings of the National Academy of Sciences en-US http://www.atypon.com/images/atypon_logo_small.gif http://www.atypon.com https://www.pnas.org/doi/abs/10.1073/pnas.2519139123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 22, June 2026. <br/>SignificanceUrinary tract infections (UTIs) are among the most common bacterial infections. Their initiation depends on the ability of uropathogenicEscherichia coli(UPEC) to adhere to bladder cells. Adhesion is mediated by FimH, a two-domain protein on ... Ultraslow conformational dynamics and catch bond formation of a bacterial adhesin revealed by a single-domain variant of FimH doi:10.1073/pnas.2519139123 2026-05-27T07:00:00Z Pearl MagalaLisa M. TuttleGianluca InterlandiLaura A. CarlucciMolly Y. MollicaMaria K. JanowskaWendy E. ThomasEvgeni V. SokurenkoRachel E. Klevitahttps://ror.org/00cvxb145Department of Biochemistry, University of Washington, Seattle, WA 98195bhttps://ror.org/00cvxb145Department of Bioengineering, University of Washington, Seattle, WA 98195chttps://ror.org/00cvxb145Department of Microbiology, University of Washington, Seattle, WA 98195 Proceedings of the National Academy of Sciences 123 22 2026-06-02T07:00:00Z 2026-06-02T07:00:00Z 10.1073/pnas.2519139123 https://www.pnas.org/doi/abs/10.1073/pnas.2519139123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2520561123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 22, June 2026. <br/>SignificanceMapping sequence–function landscape of target protein is fundamental to protein engineering and to a deeper understanding of protein function. While the effect of a single mutation is often studied, the impact of combining multiple mutations ... Navigating high-order protein fitness landscapes via deep learning on directed evolution trajectories doi:10.1073/pnas.2520561123 2026-05-26T07:00:00Z Chengzhi SongLiang MaLingfeng XueYingfan XuQihan ZhangYuxi LiuChen SongYihan LinaCenter for Quantitative Biology and Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, ChinabThe Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, ChinacPeking University Chengdu Academy for Advanced Interdisciplinary Biotechnologies, Chengdu, Sichuan 610213, China Proceedings of the National Academy of Sciences 123 22 2026-06-02T07:00:00Z 2026-06-02T07:00:00Z 10.1073/pnas.2520561123 https://www.pnas.org/doi/abs/10.1073/pnas.2520561123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2531932123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 22, June 2026. <br/>SignificanceProteins undergo two fundamental types of phase transitions—amyloid aggregation and liquid–liquid phase separation (LLPS)—that shape cellular organization and contribute to diseases ranging from Alzheimer’s to cancer. While these processes are ... amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome doi:10.1073/pnas.2531932123 2026-05-26T07:00:00Z Samuel LoboLeif GriemM. Scott ShellJoan-Emma Sheaahttps://ror.org/02t274463Department of Chemical Engineering, University of California, Santa Barbara, CA 93106bhttps://ror.org/02t274463Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106chttps://ror.org/02t274463Department of Physics, University of California, Santa Barbara, CA 93106 Proceedings of the National Academy of Sciences 123 22 2026-06-02T07:00:00Z 2026-06-02T07:00:00Z 10.1073/pnas.2531932123 https://www.pnas.org/doi/abs/10.1073/pnas.2531932123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2609796123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 22, June 2026. <br/>SignificanceStructural maintenance of chromosomes complexes such as cohesin and condensin actively organize genomes by extruding DNA loops. A key property of these motors is their processivity–the distance and duration over which loop extrusion persists. ... Theory of chromosome structural dynamics by processive loop extrusion doi:10.1073/pnas.2609796123 2026-05-28T07:00:00Z Zhiyu CaoChaoqun DuZhonghuai HouPeter G. WolynesaCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005bDepartment of Chemical Physics, University of Science and Technology of China, Hefei, Anhui 230026, ChinacDepartment of Chemistry, Rice University, Houston, TX 77005dDepartment of Physics, Rice University, Houston, TX 77005 Proceedings of the National Academy of Sciences 123 22 2026-06-02T07:00:00Z 2026-06-02T07:00:00Z 10.1073/pnas.2609796123 https://www.pnas.org/doi/abs/10.1073/pnas.2609796123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2523342123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 21, May 2026. <br/>SignificanceThe totality of the protein–carbohydrate interactome remains elusive, in part due to the inability to directly probe a proteome versus a glycome in a high throughput manner. Here we show a high-throughput methodology to predict protein–... Predictions from deep learning propose substantial protein–carbohydrate interplay doi:10.1073/pnas.2523342123 2026-05-18T07:00:00Z Samuel W. CannerRonald L. SchnaarJeffrey J. GrayaProgram in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218bDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21287cDepartment of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21287dDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD 21218 Proceedings of the National Academy of Sciences 123 21 2026-05-26T07:00:00Z 2026-05-26T07:00:00Z 10.1073/pnas.2523342123 https://www.pnas.org/doi/abs/10.1073/pnas.2523342123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2524201123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 21, May 2026. <br/>SignificancePredicting protein interactions and functions is a key challenge in biology. Although deep learning-based language models are advancing the analysis of individual protein sequences and of genomic neighborhoods, they struggle to capture ... ProteomeLM: A proteome-scale language model enables accurate and rapid prediction of protein–protein interactions and gene essentiality across taxa doi:10.1073/pnas.2524201123 2026-05-20T07:00:00Z Cyril MalbrankeGionata Paolo ZalaffiAnne-Florence Bitbolahttps://ror.org/02s376052Institute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne CH-1015, Switzerlandbhttps://ror.org/002n09z45Swiss Institute of Bioinformatics, Lausanne CH-1015, Switzerland Proceedings of the National Academy of Sciences 123 21 2026-05-26T07:00:00Z 2026-05-26T07:00:00Z 10.1073/pnas.2524201123 https://www.pnas.org/doi/abs/10.1073/pnas.2524201123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2528603123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 21, May 2026. <br/>SignificanceDuring early human development, epithelial tissues must undergo large and rapid shape changes without rupturing or losing function. How epithelia tolerate such extreme deformations while maintaining barrier integrity remains unclear. Here, we ... Reversible superdeformability of hiPSC epithelial cortinoids doi:10.1073/pnas.2528603123 2026-05-18T07:00:00Z Anirban JanaJustin TauberAdeline BoyreauBasile GurchenkovGaëlle RecherMaxime FeyeuxKevin AlessandriPierre NassoyL. MahadevanaLaboratoire Photonique Numérique et Nanosciences, University of Bordeaux, Talence 33400, FrancebTreefrog Therapeutics, Pessac 33600, Francechttps://ror.org/03vek6s52School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138dInstitut d’Optique Graduate School, UMR 5298, CNRS, Talence 33400, Franceehttps://ror.org/03vek6s52Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA 02138fhttps://ror.org/03vek6s52Department of Physics, Harvard University, Cambridge, MA 02138 Proceedings of the National Academy of Sciences 123 21 2026-05-26T07:00:00Z 2026-05-26T07:00:00Z 10.1073/pnas.2528603123 https://www.pnas.org/doi/abs/10.1073/pnas.2528603123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2528689123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 21, May 2026. <br/>SignificanceThe proapoptotic activity of apoptosis-inducing factor (AIF) before its release is explored using label-free Raman spectroscopy and in situ Raman imaging. Electron transfer and interactional details between AIF and cytochrome c are revealed, ... Apoptosis-inducing factor starts its activity within mitochondria revealed by in situ vibrational probes doi:10.1073/pnas.2528689123 2026-05-20T07:00:00Z Jinyu ZhuYi LiaoMengfan FengLi SongWei LiLinjun CaiXiao Xia HanaState Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun 130012, People’s Republic of Chinabhttps://ror.org/00js3aw79National Engineering Laboratory for Acquired Immunodeficiency Syndrome Vaccine, School of Life Sciences, Jilin University, Changchun 130012, People’s Republic of China Proceedings of the National Academy of Sciences 123 21 2026-05-26T07:00:00Z 2026-05-26T07:00:00Z 10.1073/pnas.2528689123 https://www.pnas.org/doi/abs/10.1073/pnas.2528689123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2534871123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 21, May 2026. <br/>SignificanceCells that migrate using blebs must rapidly expand their plasma membrane, yet how they reorganize membrane curvature and proteins during this process has remained unclear. Here, we identify a previously unrecognized membrane structure, the sub-... Bleb expansion requires transient membrane invaginations that sequester curvature-preferring proteins doi:10.1073/pnas.2534871123 2026-05-20T07:00:00Z Yuki MaekawaSaori R. YoshiiNoboru MizushimaJunichi Ikenouchiahttps://ror.org/00p4k0j84Department of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582, Japanbhttps://ror.org/057zh3y96Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japanchttps://ror.org/057zh3y96International Research Center for Neurointelligence, The University of Tokyo Institute for Advanced Study, The University of Tokyo, Tokyo 113-0033, Japan Proceedings of the National Academy of Sciences 123 21 2026-05-26T07:00:00Z 2026-05-26T07:00:00Z 10.1073/pnas.2534871123 https://www.pnas.org/doi/abs/10.1073/pnas.2534871123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2604562123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 21, May 2026. <br/>SignificanceMuch of the human proteome lacks stable structure and consists of intrinsically disordered regions (IDRs). IDRs have key roles in cellular signaling, gene expression, and cellular organization, but their rapid sequence evolution has made them ... A functional map of the human intrinsically disordered proteome doi:10.1073/pnas.2604562123 2026-05-18T07:00:00Z Iva PritišanacT. Reid AldersonĐesika KolarićTaraneh ZarinShuting XieAlex LuAqsa AlamAbdullah MaqsoodJi-Young YounJulie D. Forman-KayAlan M. Mosesahttps://ror.org/03dbr7087Department of Cell and Systems Biology, University of Toronto, Toronto, ON M5S 3G5, Canadabhttps://ror.org/057q4rt57Program in Molecular Medicine, The Hospital for Sick Children, Toronto, ON M5G 0A4, CanadacDepartment of Medicinal Chemistry, Otto Loewi Research Center, Medical University of Graz, Graz 8043, Austriadhttps://ror.org/00kg2yq63Helmholtz Munich, Computational Health Center, Institute of Computational Biology, Neuherberg 85764, GermanyeHelmholtz Munich, Molecular Targets and Therapeutics Center, Institute of Structural Biology, Neuherberg 85764, Germanyfhttps://ror.org/02kkvpp62Technical University of Munich School of Natural Sciences, Department of Bioscience, Bavarian Nuclear Magnetic Resonance Center, Technical University of Munich, Garching 85747, Germanyghttps://ror.org/03dbr7087Department of Computer Science, University of Toronto, Toronto, ON M5S 2E4, Canadahhttps://ror.org/03dbr7087Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canadaihttps://ror.org/03dbr7087Department of Biochemistry, The University of Toronto, Toronto, ON M5S 1A8, Canada Proceedings of the National Academy of Sciences 123 21 2026-05-26T07:00:00Z 2026-05-26T07:00:00Z 10.1073/pnas.2604562123 https://www.pnas.org/doi/abs/10.1073/pnas.2604562123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2527963123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 20, May 2026. <br/>SignificanceProgrammed cell death, or apoptosis, is a fundamental process that eliminates damaged cells. However, cancer cells often evade this process by overexpressing antiapoptotic Bcl-2 family proteins, which neutralize their proapoptotic ... Structural and dynamic basis of indirect apoptosis inhibition by Bcl-xL: A case study with Bid doi:10.1073/pnas.2527963123 2026-05-11T07:00:00Z Christina ElsnerAnton HankeOscar VadasFrancesco Luigi GervasioEnrica BordignonaDepartment of Physical Chemistry, University of Geneva, Geneva 1211, SwitzerlandbDepartment of Pharmaceutical Sciences, University of Geneva, Geneva 1211, SwitzerlandcSwiss institute of Bioinformatics, University of GenevadDepartment of Microbiology and Molecular Medicine, University of GenevaeDepartment of Chemistry, University College London, London WC1E 6BT, United Kingdom Proceedings of the National Academy of Sciences 123 20 2026-05-19T07:00:00Z 2026-05-19T07:00:00Z 10.1073/pnas.2527963123 https://www.pnas.org/doi/abs/10.1073/pnas.2527963123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2529979123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 20, May 2026. <br/>SignificanceProteins and other biomolecules operate through transient, nonequilibrium intermediates that are crucial for function. Even folding, by which proteins reach native shapes despite astronomical possibilities posed by Levinthal’s paradox, ... NEXT-FRET maps nonequilibrium rerouting of Escherichia coli maltose-binding protein folding by its signal peptide and chaperones doi:10.1073/pnas.2529979123 2026-05-12T07:00:00Z Chara SarafoglouAndreas KofidisMarijn de BoerMikis MylonakisKostas MavrakisGiannis ZacharakisYannis PantazisGiorgos GouridisaLaboratory of Dynamic Structural Biology, Structural Biology and Biophysics Division, Institute of Molecular Biology and Biotechnology (IMBB-Foundation for Research and Technology-Hellas), Heraklion-Crete 70013, Greecebhttps://ror.org/00dr28g20Department of Biology, University of Crete, Heraklion-Crete 70013, GreececInstitute of Applied and Computational Mathematics, Foundation for Research and Technology—Hellas, Heraklion-Crete 70013, Greecedhttps://ror.org/00dr28g20Department of Computer Science, University of Crete, Heraklion-Crete 70013, Greeceehttps://ror.org/012p63287Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Groningen 9747 AG, The NetherlandsfLaboratory for Biophotonics and molecular imaging, Institute of Electronic Structure and Lasers (IESL-Foundation for Research and Technology-Hellas), Heraklion-Crete 70013, GreecegKymatonics Private Company, Heraklion-Crete 70013, Greece Proceedings of the National Academy of Sciences 123 20 2026-05-19T07:00:00Z 2026-05-19T07:00:00Z 10.1073/pnas.2529979123 https://www.pnas.org/doi/abs/10.1073/pnas.2529979123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2504793123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 19, May 2026. <br/>SignificanceOur work reveals how the D614G mutation in the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein reshapes its internal communication pathways and speeds up receptor binding domain (RBD) opening, providing mechanistic ... D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes doi:10.1073/pnas.2504793123 2026-05-08T07:00:00Z Fiona L. KearnsAnthony T. BogettiCarla Calvó-TusellMac Kevin E. BrazaLorenzo CasalinoAmanda J. GrammSean BraetMia A. RosenfeldHarinda RajapakshaBryan BarkerGanesh AnandLillian T. ChongSurl-Hee AhnRommie E. AmaroaDepartment of Molecular Biology, University of California San Diego, La Jolla, CA 92093-0340bDepartment of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260cDepartment of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA 92093-0340dDepartment of Chemistry, Pennsylvania State University, University Park, PA 16802eOracle for Research, Oracle Cloud, Austin, TX 78741fDepartment of Chemical Engineering, University of California Davis, Davis, CA 95616 Proceedings of the National Academy of Sciences 123 19 2026-05-12T07:00:00Z 2026-05-12T07:00:00Z 10.1073/pnas.2504793123 https://www.pnas.org/doi/abs/10.1073/pnas.2504793123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2528758123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 19, May 2026. <br/>SignificanceUnderstanding the structure of biomolecules is key to explaining their function. Cryoelectron microscopy is a method for reconstructing the electrostatic potential distribution of a biological macromolecule, a quantity which contains ... Measurement of atomic scattering factors by cryoelectron microscopy doi:10.1073/pnas.2528758123 2026-05-08T07:00:00Z Alexander ShtyrovHugh WilsonDaria SlowikKeitaro YamashitaJade LiMarcin WojdyrShaoxia ChenGreg McMullanJude M. ShortChristopher J. RussoRichard HendersonGarib N. MurshudovaMRC Laboratory of Molecular Biology, Structural Studies Division, Cambridge CB2 0QH, United KingdombStructural Biology Division, Research Center for Advanced Science and Technology, The University of Tokyo, Meguro-ku 153-8904, Tokyo, JapancGlobal Phasing Limited (United Kingdom), Cambridge CB3 0AX, United Kingdom Proceedings of the National Academy of Sciences 123 19 2026-05-12T07:00:00Z 2026-05-12T07:00:00Z 10.1073/pnas.2528758123 https://www.pnas.org/doi/abs/10.1073/pnas.2528758123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2529856123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 19, May 2026. <br/>SignificanceRibonucleotide reductases (RNRs) are ancient enzymes responsible for the synthesis of deoxyribonucleotides from ribonucleotides. RNRs catalyze this reaction via a long-range proton-coupled electron transfer (PCET) process, involving the ... Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase doi:10.1073/pnas.2529856123 2026-05-07T07:00:00Z Abhishek SirohiwalJuliane JohnYury KutinRohit KumarFederico BasergaVivek SrinivasHugo LebretteMaximilian C. PöverleinAna P. Gamiz-HernandezJoachim HeberleMüge KasanmascheffMartin HögbomVille R. I. KailaaDepartment of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm 10691, SwedenbDepartment of Inorganic and Physical Chemistry, Division of Chemical Sciences, Indian Institute of Science, Bangalore 560012, IndiacDepartment of Chemistry and Chemical Biology, Technical University Dortmund, Faculty for Chemistry and Chemical Biology, Dortmund 44227, GermanydExperimental Molecular Biophysics, Department of Physics, Freie Universität Berlin, Berlin 14195, GermanyeLaboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative, CNRS, Université de Toulouse, Toulouse 31062, France Proceedings of the National Academy of Sciences 123 19 2026-05-12T07:00:00Z 2026-05-12T07:00:00Z 10.1073/pnas.2529856123 https://www.pnas.org/doi/abs/10.1073/pnas.2529856123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2531363123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 19, May 2026. <br/>SignificanceThe light-harvesting complex 2 (LH2) antenna of purple bacteria is a model system for photosynthetic light harvesting. The discovery of its delocalized excited states established a picture in which delocalization and associated rapid energy ... Trade-offs between light absorption and energy transfer in a marine light-harvesting complex 2 doi:10.1073/pnas.2531363123 2026-05-07T07:00:00Z Graham P. SchmidtDihao WangAmala PhadkuleChern ChuangMike ReppertGabriela S. Schlau-CohenaDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139bDepartment of Chemistry, Purdue University, West Lafayette, IN 47907cDepartment of Chemistry, University of Nevada, Las Vegas, NV 89154dDepartment of Biochemistry, University of Nevada, Las Vegas, NV 89154 Proceedings of the National Academy of Sciences 123 19 2026-05-12T07:00:00Z 2026-05-12T07:00:00Z 10.1073/pnas.2531363123 https://www.pnas.org/doi/abs/10.1073/pnas.2531363123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2426811123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 18, May 2026. <br/>SignificanceThis study investigates the structural biology of the necroptotic pathway, an understudied programmed cell death mechanism that plays a crucial role in innate immunity and has implications for infectious diseases, cell cycle regulation, and ... Structural studies of an antinecroptosis viral:human functional heteroamyloid M45:RIPK3 using SSNMR doi:10.1073/pnas.2426811123 2026-04-27T07:00:00Z Chengming HeNikhil R. VargheseEric G. KeelerChi L. L. PhamTeng XieBrayden WilliamsStephan TetterCrystal SemaanKaryn L. WildeSimon H. J. BrownJames C. BouwerYann GambinEmma SiereckiMegan SteainRuhong ZhouMargaret SundeAnn E. McDermottaDepartment of Chemistry, Columbia University, New York, NY 10027bSchool of Medical Sciences and Sydney Nano Institute, University of Sydney, Sydney, NSW 2006, AustraliacMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United KingdomdInstitute of Quantitative Biology, Zhejiang University, Hangzhou 310003, ChinaeNational Deuteration Facility, Australian Nuclear Science and Technology Organization, Sydney, NSW 2234, AustraliafAustralian Research Council Centre for Cryo-electron Microscopy of Membrane Proteins, University of Wollongong, Wollongong, NSW 2522, AustraliagDepartment of Molecular Medicine and European Molecular Biology Laboratory Australia Node in Single Molecule Science, School of Biomedical Sciences, University of New South Wales, Sydney, NSW 2052, Australia Proceedings of the National Academy of Sciences 123 18 2026-05-05T07:00:00Z 2026-05-05T07:00:00Z 10.1073/pnas.2426811123 https://www.pnas.org/doi/abs/10.1073/pnas.2426811123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2529837123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 18, May 2026. <br/>SignificanceElucidation of the structure of PrPSchas opened the possibility to understand propagation of this quintessential prion. However, PrPScis a standard amyloid made of flat stacked monomers. Therefore, its templating surface can easily direct ... Exploring PrPC unfolding as a critical step preceding its refolding in the context of PrPSc propagation doi:10.1073/pnas.2529837123 2026-04-29T07:00:00Z Sanaz SabzeheiMarta RigoliRaúl CacheiroIria Díaz-AriasHasier ErañaRubén P. LagoArcadio GuerraHuman RezaeiJoaquín CastillaEmiliano BiasiniVíctor M. Sánchez-PedregalManuel Martín-PastorJesús R. RequenaaCenter for Research in Molecular Medicine and Chronic Diseases and Department of Medical Sciences, University of Santiago de Compostela-Instituto de Investigación Sanitaria de Santiago, Santiago de Compostela 15782, Spainbhttps://ror.org/05trd4x28Department of Cellular, Computational and Integrative Biology, University of Trento, Povo, TN 38123, Italychttps://ror.org/02x5c5y60Asociación Centro de Investigación Cooperativa en Biociencias, Basque Research and Technology Alliance, Prion Research Lab, Derio 48160, SpaindAtlas Molecular Pharma S. L. Bizkaia Technology Park, Derio 48160, SpaineCentro de Investigación Biomédica en Red de Enfermedades Infecciosas, Carlos III National Health Institute, Madrid 28029, SpainfCenter for Research in Biological Chemistry and Molecular Materials, University of Santiago de Compostela, Santiago de Compostela 15782, SpaingUniversité Paris-Saclay, Institut National de Recherche pour l‘Agriculture, l‘Alimentation et l‘Environnement, Université Versailles-Saint Quentin, Unité de Virologie et d‘Immunologie Moléculaires, Jouy-en-Josas 78352, Francehhttps://ror.org/01cc3fy72Ikerbasque, Basque Foundation for Science, Bilbao 48009, Spainihttps://ror.org/030eybx10Department of Organic Chemistry, University of Santiago de Compostela, Santiago de Compostela 15782, Spainjhttps://ror.org/030eybx10Unidade de Resonancia Magnética, University of Santiago de Compostela, Santiago de Compostela 15782, Spain Proceedings of the National Academy of Sciences 123 18 2026-05-05T07:00:00Z 2026-05-05T07:00:00Z 10.1073/pnas.2529837123 https://www.pnas.org/doi/abs/10.1073/pnas.2529837123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2532989123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 18, May 2026. <br/>SignificanceInfluenza B infections contribute to seasonal flu each year, producing illness severity and hospitalization rates comparable to those of influenza A infections. We isolated a panel of broadly neutralizing antibodies against influenza B strains ... Broad neutralization of influenza B hemagglutinin antibodies via receptor mimicry and glycan engagement doi:10.1073/pnas.2532989123 2026-04-30T07:00:00Z Kuan-Ying A. HuangHong Thuy Vy NguyenYi-Yin ChenKai-Jung WuPo-Hsien HsuYo-Min LiuTzou-Yien LinChe MaaGraduate Institute of Immunology and Department of Pediatrics, National Taiwan University Hospital, College of Medicine, National Taiwan University, Taipei 100225, TaiwanbGenomics Research Center, Academia Sinica, Taipei 115201, TaiwancGraduate Institute of Life Sciences, College of Biomedical Sciences, National Defense Medical University, Taipei 114201, TaiwandDivision of Infectious Diseases, Department of Pediatrics, Chang Gung Memorial Hospital and College of Medicine, Chang Gung University, Taoyuan 333323, Taiwan Proceedings of the National Academy of Sciences 123 18 2026-05-05T07:00:00Z 2026-05-05T07:00:00Z 10.1073/pnas.2532989123 https://www.pnas.org/doi/abs/10.1073/pnas.2532989123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2533138123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 18, May 2026. <br/>SignificanceInsects were the first organisms to evolve flight and have since become the most abundant species on Earth. However, the lack of well-defined flight traits and predictive theory has made it difficult to quantify the evolution of traits across ... Stable flapping flight in morphological space: Model, simulation, and explicit stability criteria doi:10.1073/pnas.2533138123 2026-05-01T07:00:00Z Owen C. WetherbeeZ. Jane Wangahttps://ror.org/05bnh6r87Department of Physics, Cornell University, Ithaca, NY 14850bhttps://ror.org/05bnh6r87Sibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY 14850 Proceedings of the National Academy of Sciences 123 18 2026-05-05T07:00:00Z 2026-05-05T07:00:00Z 10.1073/pnas.2533138123 https://www.pnas.org/doi/abs/10.1073/pnas.2533138123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2533456123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 18, May 2026. <br/>SignificanceMultiple porcine deltacoronavirus (PDCoV) spillovers occurred in Haiti and there are currently no vaccines or therapeutics approved for use in humans. We computationally designed PDCoV miniprotein inhibitors and identified one (MB11) that ... Computational design of an ultrapotent deltacoronavirus miniprotein inhibitor doi:10.1073/pnas.2533456123 2026-04-29T07:00:00Z Nathan G. AveryCourtney N. YoshiyamaAshley L. TaylorYoung-Jun ParkDaniel AsarnowLisa PerruzzaJack T. BrownDavide CortiFabio BenigniTyler N. StarrDavid VeesleraDepartment of Biochemistry, University of Washington, Seattle, WA 98195bDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112cHHMI, University of Washington, Seattle, WA 98195dHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, Bellinzona 6500, Switzerland Proceedings of the National Academy of Sciences 123 18 2026-05-05T07:00:00Z 2026-05-05T07:00:00Z 10.1073/pnas.2533456123 https://www.pnas.org/doi/abs/10.1073/pnas.2533456123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2533975123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 18, May 2026. <br/>SignificanceChemokine receptor CCR7 directs immune cell migration by activating distinct signaling pathways in response to CCL19 and CCL21, a phenomenon known as biased agonism. The structural basis for this divergence has remained unclear. By combining ... Structural insights into biased signaling at chemokine receptor CCR7 doi:10.1073/pnas.2533975123 2026-04-29T07:00:00Z Kotaro TanakaKouki NishikawaYuki ShiimuraYoshinori FujiyoshiNaotaka Tsutsumiahttps://ror.org/05dqf9946Cellular and Structural Physiology Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Bunkyo, Tokyo 113-8510, Japanbhttps://ror.org/00qg0kr10Joint Research Course for Advanced Biomolecular Characterization, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Tokyo 183-8509, JapancDivision of Molecular Genetics, Institute of Life Science, Kurume University, Fukuoka 830-0011, Japandhttps://ror.org/02kpeqv85Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan Proceedings of the National Academy of Sciences 123 18 2026-05-05T07:00:00Z 2026-05-05T07:00:00Z 10.1073/pnas.2533975123 https://www.pnas.org/doi/abs/10.1073/pnas.2533975123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2601748123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 18, May 2026. <br/>SignificanceMutations in transmembrane domains (TMDs) of cytokine and immune receptors often cause aberrant, ligand-independent signaling linked to diverse malignancies, but the mechanisms are largely unknown. This paper reveals an oncogenic mutation ... Structural rewiring of IL-7R dimerization by an oncogenic transmembrane mutation can be reversed by rational design doi:10.1073/pnas.2601748123 2026-04-28T07:00:00Z Qian WangMin ChenAsma LasramSaana VihuriAngela Z. ChouWeixin BianZhiming DaiOuti HaapanenGiray EnkaviChristoph PollmannIlpo VattulainenTiantian CaiJacob PiehlerJames J. ChouaInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, ChinabState Key Laboratory of Chemical Biology, Chinese Academy of Sciences, Shanghai 201203, ChinacDepartment of Biology/Chemistry and Center for Cellular Nanoanalytics, Osnabrück University, Osnabrück 49076, GermanydDepartment of Physics, University of Helsinki, Helsinki 00014, FinlandeUniversity of Chinese Academy of Sciences, Beijing 101408, ChinafInstitute of Quantum Sensing, Institute of Fundamental and Transdisciplinary Research, Zhejiang University, Hangzhou, Zhejiang 310027, China Proceedings of the National Academy of Sciences 123 18 2026-05-05T07:00:00Z 2026-05-05T07:00:00Z 10.1073/pnas.2601748123 https://www.pnas.org/doi/abs/10.1073/pnas.2601748123?af=R