Chenguang Yang, Dongfei Ma, Shuxin Hu, Ming Li, Ying Lu
{"title":"利用单分子成像技术实时分析膜蛋白插入的纳米级动态。","authors":"Chenguang Yang, Dongfei Ma, Shuxin Hu, Ming Li, Ying Lu","doi":"10.52601/bpr.2024.240024","DOIUrl":null,"url":null,"abstract":"<p><p>Membrane proteins often need to be inserted into or attached to the cell membrane to perform their functions. Understanding their transmembrane topology and conformational dynamics during insertion is crucial for elucidating their roles. However, it remains challenging to monitor nanoscale changes in the insertion depth of individual proteins in membranes. Here, we introduce two single-molecule imaging methods, SIFA and LipoFRET, designed for <i>in vitro</i> observation of the nanoscale architecture of membrane proteins within membranes. These methods have demonstrated their efficacy in studying biomolecules interacting with bio-membranes with sub-nanometer precision.</p>","PeriodicalId":93906,"journal":{"name":"Biophysics reports","volume":"10 6","pages":"369-376"},"PeriodicalIF":0.0000,"publicationDate":"2024-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11693496/pdf/","citationCount":"0","resultStr":"{\"title\":\"Real-time analysis of nanoscale dynamics in membrane protein insertion via single-molecule imaging.\",\"authors\":\"Chenguang Yang, Dongfei Ma, Shuxin Hu, Ming Li, Ying Lu\",\"doi\":\"10.52601/bpr.2024.240024\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Membrane proteins often need to be inserted into or attached to the cell membrane to perform their functions. Understanding their transmembrane topology and conformational dynamics during insertion is crucial for elucidating their roles. However, it remains challenging to monitor nanoscale changes in the insertion depth of individual proteins in membranes. Here, we introduce two single-molecule imaging methods, SIFA and LipoFRET, designed for <i>in vitro</i> observation of the nanoscale architecture of membrane proteins within membranes. These methods have demonstrated their efficacy in studying biomolecules interacting with bio-membranes with sub-nanometer precision.</p>\",\"PeriodicalId\":93906,\"journal\":{\"name\":\"Biophysics reports\",\"volume\":\"10 6\",\"pages\":\"369-376\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-12-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11693496/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biophysics reports\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.52601/bpr.2024.240024\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysics reports","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.52601/bpr.2024.240024","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Real-time analysis of nanoscale dynamics in membrane protein insertion via single-molecule imaging.
Membrane proteins often need to be inserted into or attached to the cell membrane to perform their functions. Understanding their transmembrane topology and conformational dynamics during insertion is crucial for elucidating their roles. However, it remains challenging to monitor nanoscale changes in the insertion depth of individual proteins in membranes. Here, we introduce two single-molecule imaging methods, SIFA and LipoFRET, designed for in vitro observation of the nanoscale architecture of membrane proteins within membranes. These methods have demonstrated their efficacy in studying biomolecules interacting with bio-membranes with sub-nanometer precision.