{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T12:31:24Z","timestamp":1787056284186,"version":"build-2736575974"},"reference-count":56,"publisher":"American Chemical Society (ACS)","issue":"16","license":[{"start":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T00:00:00Z","timestamp":1785369600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T00:00:00Z","timestamp":1785369600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T00:00:00Z","timestamp":1785369600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology, Ministry of Science and Technology, India","doi-asserted-by":"publisher","award":["HRD-20\/1\/2024-HRD-DBT"],"award-info":[{"award-number":["HRD-20\/1\/2024-HRD-DBT"]}],"id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001843","name":"Science and Engineering Research Board","doi-asserted-by":"publisher","award":["EMR\/2016\/001774"],"award-info":[{"award-number":["EMR\/2016\/001774"]}],"id":[{"id":"10.13039\/501100001843","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001843","name":"Science and Engineering Research Board","doi-asserted-by":"publisher","award":["SERB\/WEA-13\/2016"],"award-info":[{"award-number":["SERB\/WEA-13\/2016"]}],"id":[{"id":"10.13039\/501100001843","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009053","name":"Wellcome Trust DBT India Alliance","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100009053","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,8,18]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Assembly energetics of transmembrane proteins occurs through the orchestrated molecular interplay of the protein\u2019s membrane partitioning free energy and the mechanical and physicochemical properties of the bilayer. While amphipathic residues help accommodate diametrically opposite forces and the steep energy gradient at the membrane\u2013water interface, the magnitude to which the intrinsic curvature and elastic energy of the bilayer regulates protein thermodynamics at the interface remains poorly understood. Here, using PagP as a model \u03b2-barrel, we compare the per-residue energetics of an interface site across membranes with(out) distinct curvature stress, lipid packing, and headgroup chemistry. In vesicles, the measured interface energetics correlates well with known free energy scales. Interestingly, unlike vesicles, we show that planar bicelles impose fundamentally distinct membrane\u2013protein coupling regimes: (i) PagP experiences altered folding with a stabilized membrane-associated intermediate and (ii) side chain transfer free energies are restructured in a residue-specific manner. Additionally, the energetics are unaffected by the presence of nonlamellar lipids. Our results reveal an unexpected dependence of partitioning energetics on both bilayer elastic energy and lipid packing defects, demonstrating how subtle changes in membrane physical properties could redirect protein folding pathways and thermodynamics. Our findings underscore the need for caution when extrapolating side chain transfer free energies from simplified model membranes to crowded, compositionally complex in vivo environments.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00283","type":"journal-article","created":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T13:19:34Z","timestamp":1785849574000},"page":"2535-2547","source":"Crossref","is-referenced-by-count":0,"title":["Bilayer Elastic\nProperties Modulate Interface Energetics\nof Transmembrane \u03b2-Barrels"],"prefix":"10.1021","volume":"65","author":[{"given":"Swadha","family":"Gupta","sequence":"first","affiliation":[{"name":"Central University of Gujarat , , Kundhela , , ,","place":["Vadodara, Gujarat, India, 391107"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1549-7550","authenticated-orcid":true,"given":"Radhakrishnan","family":"Mahalakshmi","sequence":"additional","affiliation":[{"name":"Krea University , , 5655 Central Expressway , , ,","place":["Sri City, Andhra Pradesh, India, 517646"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,7,30]]},"reference":[{"key":"2026081808123706900_cit1","doi-asserted-by":"publisher","first-page":"4619","DOI":"10.1021\/acs.chemrev.5c00902","article-title":"Decoding Outer\nMembrane beta-Barrels: From Structural Curiosity to Engineered Nanotherapeutics","volume":"126","author":"Mahalakshmi","year":"2026","journal-title":"Chem. Rev."},{"key":"2026081808123706900_cit2","doi-asserted-by":"publisher","first-page":"1012","DOI":"10.1126\/science.653353","article-title":"The hydrophobic\neffect and the organization of living matter","volume":"200","author":"Tanford","year":"1978","journal-title":"Science"},{"key":"2026081808123706900_cit3","doi-asserted-by":"publisher","first-page":"172","DOI":"10.1038\/nature13419","article-title":"Membrane\nproteins\nbind lipids selectively to modulate their structure and function","volume":"510","author":"Laganowsky","year":"2014","journal-title":"Nature"},{"key":"2026081808123706900_cit4","doi-asserted-by":"publisher","first-page":"4285","DOI":"10.1073\/pnas.1212527110","article-title":"Membrane\nprotein thermodynamic stability may serve as the energy sink for sorting\nin the periplasm","volume":"110","author":"Moon","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026081808123706900_cit5","doi-asserted-by":"publisher","first-page":"10174","DOI":"10.1073\/pnas.1103979108","article-title":"Side-chain hydrophobicity scale derived\nfrom transmembrane\nprotein folding into lipid bilayers","volume":"108","author":"Moon","year":"2011","journal-title":"Proc. Natl.\nAcad. Sci. U.S.A."},{"key":"2026081808123706900_cit6","doi-asserted-by":"publisher","first-page":"12351","DOI":"10.1074\/jbc.M117.789446","article-title":"Energetics\nof side-chain partitioning of beta-signal residues in unassisted folding\nof a transmembrane beta-barrel protein","volume":"292","author":"Iyer","year":"2017","journal-title":"J. Biol.\nChem."},{"key":"2026081808123706900_cit7","doi-asserted-by":"publisher","first-page":"2467","DOI":"10.1016\/j.bbamem.2017.09.020","article-title":"Transmembrane\nbeta-barrels: Evolution, folding and\nenergetics","volume":"1859","author":"Chaturvedi","year":"2017","journal-title":"Biochim. Biophys. Acta, Biomembr."},{"key":"2026081808123706900_cit8","doi-asserted-by":"publisher","first-page":"951","DOI":"10.1016\/j.bbamem.2011.12.029","article-title":"Progress\nin understanding the role of lipids in membrane protein folding","volume":"1818","author":"Mitchell","year":"2012","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"2026081808123706900_cit9","doi-asserted-by":"publisher","first-page":"10340","DOI":"10.1074\/jbc.REV120.011473","article-title":"Role of the lipid\nbilayer in outer\nmembrane protein folding in Gram-negative bacteria","volume":"295","author":"Horne","year":"2020","journal-title":"J. Biol. Chem."},{"key":"2026081808123706900_cit10","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1016\/j.sbi.2021.11.013","article-title":"Untangling the complexity of membrane\nprotein folding","volume":"72","author":"Hong","year":"2022","journal-title":"Curr. Opin. Struct. 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Int.\nEd."},{"key":"2026081808123706900_cit14","doi-asserted-by":"publisher","first-page":"2107","DOI":"10.1093\/emboj\/21.9.2107","article-title":"A polytopic\nmembrane protein displays\na reversible topology dependent on membrane lipid composition","volume":"21","author":"Bogdanov","year":"2002","journal-title":"EMBO J."},{"key":"2026081808123706900_cit15","doi-asserted-by":"publisher","first-page":"7373","DOI":"10.1038\/s41467-022-35202-8","article-title":"Membrane-mediated protein interactions\ndrive membrane protein organization","volume":"13","author":"Jiang","year":"2022","journal-title":"Nat. Commun."},{"key":"2026081808123706900_cit16","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1146\/annurev.bb.22.060193.001045","article-title":"Models of lipid-protein interactions\nin membranes","volume":"22","author":"Mouritsen","year":"1993","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"2026081808123706900_cit17","doi-asserted-by":"publisher","first-page":"5712","DOI":"10.1021\/acs.biochem.5b00543","article-title":"Residue-Dependent\nThermodynamic Cost and Barrel Plasticity\nBalances Activity in the PhoPQ-Activated Enzyme PagP of Salmonella\ntyphimurium","volume":"54","author":"Iyer","year":"2015","journal-title":"Biochemistry"},{"key":"2026081808123706900_cit18","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1038\/nrm2977","article-title":"Revitalizing membrane rafts: new\ntools and insights","volume":"11","author":"Simons","year":"2010","journal-title":"Nat. Rev. Mol. 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Rep."},{"key":"2026081808123706900_cit22","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1016\/j.bbamem.2011.10.026","article-title":"The role of membrane thickness in\ncharged protein-lipid interactions","volume":"1818","author":"Li","year":"2012","journal-title":"Biochim.\nBiophys. Acta Gen. Subj."},{"key":"2026081808123706900_cit23","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1016\/S0968-0004(00)01626-1","article-title":"How proteins\nadapt to a membrane-water interface","volume":"25","author":"Killian","year":"2000","journal-title":"Trends\nBiochem. Sci."},{"key":"2026081808123706900_cit24","doi-asserted-by":"publisher","first-page":"15427","DOI":"10.1073\/pnas.1007455107","article-title":"Amphiphile regulation\nof ion channel function by changes in the bilayer spring constant","volume":"107","author":"Lundbaek","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026081808123706900_cit25","doi-asserted-by":"publisher","first-page":"15831","DOI":"10.1021\/acs.jpcb.5b08463","article-title":"Bicelles and Other Membrane Mimics: Comparison of Structure,\nProperties, and Dynamics from MD Simulations","volume":"119","author":"Vestergaard","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"2026081808123706900_cit26","doi-asserted-by":"publisher","first-page":"13560","DOI":"10.1073\/pnas.212344499","article-title":"Solution\nstructure and dynamics of the outer membrane enzyme PagP by NMR","volume":"99","author":"Hwang","year":"2002","journal-title":"Proc. Natl. Acad. Sci. 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Struct.\nBiol."},{"key":"2026081808123706900_cit30","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1038\/nature03216","article-title":"Recognition\nof transmembrane helices by the endoplasmic reticulum translocon","volume":"433","author":"Hessa","year":"2005","journal-title":"Nature"},{"key":"2026081808123706900_cit31","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1016\/j.bpj.2019.05.024","article-title":"Hydrophobic\nCharacteristic Is Energetically Preferred\nfor Cysteine in a Model Membrane Protein","volume":"117","author":"Iyer","year":"2019","journal-title":"Biophys.\nJ."},{"key":"2026081808123706900_cit32","doi-asserted-by":"publisher","first-page":"4099","DOI":"10.1073\/pnas.0911904107","article-title":"The transition state\nfor folding of an outer membrane protein","volume":"107","author":"Huysmans","year":"2010","journal-title":"Proc.\nNatl. Acad. Sci. U.S.A."},{"key":"2026081808123706900_cit33","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1007\/978-1-0716-0724-4_10","article-title":"Determining the\nFree Energies of Outer Membrane Proteins in Lipid Bilayers","volume":"2168","author":"Huysmans","year":"2020","journal-title":"Methods Mol. Biol."},{"key":"2026081808123706900_cit34","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1021\/acs.biochem.9b00731","article-title":"Molecular\nSwitch between Structural\nCompaction and Thermodynamic Stability by the Xxx-Pro Interface in\nTransmembrane beta-Barrels","volume":"59","author":"Iyer","year":"2020","journal-title":"Biochemistry"},{"key":"2026081808123706900_cit35","doi-asserted-by":"publisher","first-page":"6669","DOI":"10.1021\/acs.biochem.8b00805","article-title":"Salvaging\nthe Thermodynamic Destabilization of Interface Histidine in Transmembrane\nbeta-Barrels","volume":"57","author":"Iyer","year":"2018","journal-title":"Biochemistry"},{"key":"2026081808123706900_cit36","doi-asserted-by":"publisher","first-page":"1545","DOI":"10.1021\/jacs.1c05964","article-title":"Engineering a Hyperstable Yersinia\npestis Outer Membrane Protein Ail Using Thermodynamic Design","volume":"144","author":"George","year":"2022","journal-title":"J. Am. Chem. Soc."},{"key":"2026081808123706900_cit37","doi-asserted-by":"publisher","first-page":"693","DOI":"10.1515\/znc-1973-11-1209","article-title":"Elastic properties\nof lipid bilayers: theory and possible experiments","volume":"28","author":"Helfrich","year":"1973","journal-title":"Z. Naturforsch., C:"},{"key":"2026081808123706900_cit38","doi-asserted-by":"publisher","first-page":"2625","DOI":"10.1016\/S0006-3495(99)77415-1","article-title":"Lipid composition\nand the lateral pressure profile in bilayers","volume":"76","author":"Cantor","year":"1999","journal-title":"Biophys. J."},{"key":"2026081808123706900_cit39","doi-asserted-by":"publisher","first-page":"6054","DOI":"10.1021\/cr300061w","article-title":"The magic of bicelles lights up membrane\nprotein structure","volume":"112","author":"Durr","year":"2012","journal-title":"Chem. Rev."},{"key":"2026081808123706900_cit40","doi-asserted-by":"publisher","first-page":"436","DOI":"10.1016\/j.jmb.2006.09.020","article-title":"E(z), a depth-dependent potential for assessing the\nenergies of insertion of amino acid side-chains into membranes: derivation\nand applications to determining the orientation of transmembrane and\ninterfacial helices","volume":"366","author":"Senes","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2026081808123706900_cit41","doi-asserted-by":"publisher","DOI":"10.7554\/elife.12125","article-title":"Mutational\nscanning reveals the determinants of protein\ninsertion and association energetics in the plasma membrane","volume":"5","author":"Elazar","year":"2016","journal-title":"eLife"},{"key":"2026081808123706900_cit42","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1016\/j.bbamem.2017.11.003","article-title":"Position-Specific\ncontribution of interface tryptophans\non membrane protein energetics","volume":"1860","author":"Chaturvedi","year":"2018","journal-title":"Biochim. Biophys.\nActa, Biomembr."},{"key":"2026081808123706900_cit43","doi-asserted-by":"publisher","first-page":"3637","DOI":"10.1021\/bi500439x","article-title":"2nd Comparisons\nof interfacial Phe, Tyr, and Trp residues\nas determinants of orientation and dynamics for GWALP transmembrane\npeptides","volume":"53","author":"Sparks","year":"2014","journal-title":"Biochemistry"},{"key":"2026081808123706900_cit44","doi-asserted-by":"publisher","first-page":"4464","DOI":"10.1016\/j.febslet.2014.10.017","article-title":"Juxtamembrane tryptophans have distinct roles in defining\nthe OmpX barrel-micelle boundary and facilitating protein-micelle\nassociation","volume":"588","author":"Chaturvedi","year":"2014","journal-title":"FEBS Lett."},{"key":"2026081808123706900_cit45","doi-asserted-by":"publisher","first-page":"2993","DOI":"10.1016\/j.bbamem.2016.09.011","article-title":"Control of human VDAC-2 scaffold\ndynamics by interfacial\ntryptophans is position specific","volume":"1858","author":"Maurya","year":"2016","journal-title":"Biochim. Biophys.\nActa Gen. Subj."},{"key":"2026081808123706900_cit46","doi-asserted-by":"publisher","first-page":"3497","DOI":"10.1021\/acschemneuro.1c00429","article-title":"Cellular Interactome of Mitochondrial\nVoltage-Dependent Anion Channels: Oligomerization and Channel (Mis)Regulation","volume":"12","author":"Khan","year":"2021","journal-title":"ACS Chem. Neurosci."},{"key":"2026081808123706900_cit47","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1039\/D0FD00065E","article-title":"Membrane electrostatics\nsensed by tryptophan anchors in hydrophobic model peptides depends\non non-aromatic interfacial amino acids: implications in hydrophobic\nmismatch","volume":"232","author":"Pal","year":"2021","journal-title":"Faraday Discuss."},{"key":"2026081808123706900_cit48","doi-asserted-by":"publisher","first-page":"16155","DOI":"10.1021\/bi0016117","article-title":"Role of aromatic residues at the\nlipid-water interface in micelle-bound bacteriophage M13 major coat\nprotein","volume":"39","author":"Yuen","year":"2000","journal-title":"Biochemistry"},{"key":"2026081808123706900_cit49","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1016\/j.sbi.2008.07.001","article-title":"Overcoming the challenges\nof membrane protein crystallography","volume":"18","author":"Carpenter","year":"2008","journal-title":"Curr. Opin.\nStruct. Biol."},{"key":"2026081808123706900_cit50","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/j.sbi.2017.01.003","article-title":"Modeling and\nsimulation of bacterial outer membranes\nand interactions with membrane proteins","volume":"43","author":"Patel","year":"2017","journal-title":"Curr.\nOpin. Struct. Biol."},{"key":"2026081808123706900_cit51","doi-asserted-by":"publisher","first-page":"5878","DOI":"10.1073\/pnas.1322473111","article-title":"Outer membrane\nbeta-barrel protein\nfolding is physically controlled by periplasmic lipid head groups\nand BamA","volume":"111","author":"Gessmann","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026081808123706900_cit52","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1016\/S0959-440X(99)80064-5","article-title":"Beta-barrel\nproteins from bacterial outer membranes: structure, function and refolding","volume":"9","author":"Buchanan","year":"1999","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2026081808123706900_cit53","doi-asserted-by":"publisher","first-page":"2669","DOI":"10.1016\/S0006-3495(96)79458-4","article-title":"Mechanism of alamethicin\ninsertion into lipid bilayers","volume":"71","author":"He","year":"1996","journal-title":"Biophys. J."},{"key":"2026081808123706900_cit54","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1146\/annurev.biophys.36.040306.132643","article-title":"2nd Bilayer thickness\nand membrane protein function:\nan energetic perspective","volume":"36","author":"Andersen","year":"2007","journal-title":"Annu. Rev. Biophys.\nBiomol. Struct."},{"key":"2026081808123706900_cit55","doi-asserted-by":"publisher","first-page":"1545","DOI":"10.1016\/j.bbamem.2008.01.015","article-title":"Protein modulation\nof lipids, and vice-versa, in membranes","volume":"1778","author":"Marsh","year":"2008","journal-title":"Biochim.\nBiophys. Acta Gen. Subj."},{"key":"2026081808123706900_cit56","doi-asserted-by":"publisher","DOI":"10.1126\/science.abc8182","article-title":"De novo design of transmembrane\nbeta barrels","volume":"371","author":"Vorobieva","year":"2021","journal-title":"Science"}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.6c00283","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/65\/16\/2535\/66334055\/acs.biochem.6c00283.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/65\/16\/2535\/66334055\/acs.biochem.6c00283.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T12:12:47Z","timestamp":1787055167000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bichaw\/article\/65\/16\/2535\/5236978\/Bilayer-Elastic-Properties-Modulate-Interface"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,30]]},"references-count":56,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2026,7,30]]},"published-print":{"date-parts":[[2026,8,18]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.biochem.6c00283","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,30]]}}}