biostudies-literatureTietjen GTUniversity of Chicago Biophysics CoreNIBIB NIH HHSDOE-BESNIAID NIH HHSUniversity of Chicago Materials Research Science and Engineering CenterArgonne National LaboratoryNational Institutes of HealthComputation Institute and the Biological Sciences Division of the University of ChicagoNIGMS NIH HHSXSEDE Compute ResourcesNIH HHSNational Science Foundation1505-1519https://www.ebi.ac.uk/biostudies/studies/S-EPMC5627149biostudies-literatureUnknown113(7)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 sensitivBiophysical journalCoupling X-Ray Reflectivity and In Silico Binding to Yield Dynamics of Membrane Recognition by Tim1.PMC5627149DMR-1420709MCB-1413613R01 AI073922R01 GM101048CHE-1346572R01-GM101048TG-MCA06N060T32 GM007183P41-GM104601T32 EB009412DE-AC02-06CH11357R01-AI073922S10 OD018495U54 GM087519P41 GM1046011S10OD018495-01U54-GM087519Tajkhorshid EBaylon JLLin BLee KYCHenderson JMMeron MHeffern CTRAdams EJTietjen GTSchlossman MLGong ZKerr DfalseCoupling X-Ray Reflectivity and In Silico Binding to Yield Dynamics of Membrane Recognition by Tim1.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 sensitiv2017-01-01T00:00:00Z2017 Oct2026-05-03T23:23:37.501Z2019-03-26T23:58:46ZS-EPMC56271492897844410.1016/j.bpj.2017.08.003