{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tietjen GT"],"funding":["University of Chicago Biophysics Core","NIBIB NIH HHS","DOE-BES","NIAID NIH HHS","University of Chicago Materials Research Science and Engineering Center","Argonne National Laboratory","National Institutes of Health","Computation Institute and the Biological Sciences Division of the University of Chicago","NIGMS NIH HHS","XSEDE Compute Resources","NIH HHS","National Science Foundation"],"pagination":["1505-1519"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5627149"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["113(7)"],"pubmed_abstract":["The dynamic nature of lipid membranes presents significant challenges with respect to understanding the molecular basis of protein/membrane interactions. Consequently, there is relatively little known about the structural mechanisms by which membrane-binding proteins might distinguish subtle variations in lipid membrane composition and/or structure. We have previously developed a multidisciplinary approach that combines molecular dynamics simulation with interfacial x-ray scattering experiments to produce an atomistic model for phosphatidylserine recognition by the immune receptor Tim4. However, this approach requires a previously determined protein crystal structure in a membrane-bound conformation. Tim1, a Tim4 homolog with distinct differences in both immunological function and sensitiv"],"journal":["Biophysical journal"],"pubmed_title":["Coupling X-Ray Reflectivity and In Silico Binding to Yield Dynamics of Membrane Recognition by Tim1."],"pmcid":["PMC5627149"],"funding_grant_id":["DMR-1420709","MCB-1413613","R01 AI073922","R01 GM101048","CHE-1346572","R01-GM101048","TG-MCA06N060","T32 GM007183","P41-GM104601","T32 EB009412","DE-AC02-06CH11357","R01-AI073922","S10 OD018495","U54 GM087519","P41 GM104601","1S10OD018495-01","U54-GM087519"],"pubmed_authors":["Tajkhorshid E","Baylon JL","Lin B","Lee KYC","Henderson JM","Meron M","Heffern CTR","Adams EJ","Tietjen GT","Schlossman ML","Gong Z","Kerr D"],"additional_accession":[]},"is_claimable":false,"name":"Coupling X-Ray Reflectivity and In Silico Binding to Yield Dynamics of Membrane Recognition by Tim1.","description":"The dynamic nature of lipid membranes presents significant challenges with respect to understanding the molecular basis of protein/membrane interactions. Consequently, there is relatively little known about the structural mechanisms by which membrane-binding proteins might distinguish subtle variations in lipid membrane composition and/or structure. We have previously developed a multidisciplinary approach that combines molecular dynamics simulation with interfacial x-ray scattering experiments to produce an atomistic model for phosphatidylserine recognition by the immune receptor Tim4. However, this approach requires a previously determined protein crystal structure in a membrane-bound conformation. Tim1, a Tim4 homolog with distinct differences in both immunological function and sensitiv","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Oct","modification":"2026-05-03T23:23:37.501Z","creation":"2019-03-26T23:58:46Z"},"accession":"S-EPMC5627149","cross_references":{"pubmed":["28978444"],"doi":["10.1016/j.bpj.2017.08.003"]}}