{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Manna P"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["eadj0807"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10745693"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(51)"],"pubmed_abstract":["Plants capture and convert solar energy in a complex network of membrane proteins. Under high light, the luminal pH drops and induces a reorganization of the protein network, particularly clustering of the major light-harvesting complex (LHCII). While the structures of the network have been resolved in exquisite detail, the thermodynamics that control the assembly and reorganization had not been determined, largely because the interaction energies of membrane proteins have been inaccessible. Here, we describe a method to quantify these energies and its application to LHCII. Using single-molecule measurements, LHCII proteoliposomes, and statistical thermodynamic modeling, we quantified the LHCII-LHCII interaction energy as ~-5 <i>k</i><sub>B</sub><i>T</i> at neutral pH and at least -7 <i>k<"],"journal":["Science advances"],"pubmed_title":["Energetic driving force for LHCII clustering in plant membranes."],"pmcid":["PMC10745693"],"funding_grant_id":["BB/W015269/1"],"pubmed_authors":["Johnson MP","Richardson KH","Manna P","Hoffmann M","Schlau-Cohen GS","Davies T"],"additional_accession":[]},"is_claimable":false,"name":"Energetic driving force for LHCII clustering in plant membranes.","description":"Plants capture and convert solar energy in a complex network of membrane proteins. Under high light, the luminal pH drops and induces a reorganization of the protein network, particularly clustering of the major light-harvesting complex (LHCII). While the structures of the network have been resolved in exquisite detail, the thermodynamics that control the assembly and reorganization had not been determined, largely because the interaction energies of membrane proteins have been inaccessible. Here, we describe a method to quantify these energies and its application to LHCII. Using single-molecule measurements, LHCII proteoliposomes, and statistical thermodynamic modeling, we quantified the LHCII-LHCII interaction energy as ~-5 <i>k</i><sub>B</sub><i>T</i> at neutral pH and at least -7 <i>k<","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2026-06-03T11:47:30.407Z","creation":"2025-04-21T15:13:42.832Z"},"accession":"S-EPMC10745693","cross_references":{"pubmed":["38134273"],"doi":["10.1126/sciadv.adj0807"]}}