{"title":"b因子和光诱导NMDA受体变构","authors":"W. Mu, Shixin Ye","doi":"10.1109/UV50937.2020.9426189","DOIUrl":null,"url":null,"abstract":"Light-sensitive protein with the light-induced allostery has great applications in bio-medical researches, which can be obtained by introducing the mutation at certain site in the protein. In the present work, we investigate the experimental data on NMDA receptors with light-sensitive mutations, and propose empirical formulas to connect the structural factors to the observable electric current change, which is the signature of the light-induced allosteric effect. We found our formulas present reasonable agreement with experimental data using the full-length structure of NMDA receptor 4tll. It can be used to predict the light-sensitive phenomena of this protein with other types of mutation. Present method can be directly extended to other proteins beyond the current 4tll.","PeriodicalId":279871,"journal":{"name":"2020 5th International Conference on Universal Village (UV)","volume":"15 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2020-10-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"B-factor and Light-induced Allostery in NMDA Receptors\",\"authors\":\"W. Mu, Shixin Ye\",\"doi\":\"10.1109/UV50937.2020.9426189\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Light-sensitive protein with the light-induced allostery has great applications in bio-medical researches, which can be obtained by introducing the mutation at certain site in the protein. In the present work, we investigate the experimental data on NMDA receptors with light-sensitive mutations, and propose empirical formulas to connect the structural factors to the observable electric current change, which is the signature of the light-induced allosteric effect. We found our formulas present reasonable agreement with experimental data using the full-length structure of NMDA receptor 4tll. It can be used to predict the light-sensitive phenomena of this protein with other types of mutation. Present method can be directly extended to other proteins beyond the current 4tll.\",\"PeriodicalId\":279871,\"journal\":{\"name\":\"2020 5th International Conference on Universal Village (UV)\",\"volume\":\"15 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2020-10-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"2020 5th International Conference on Universal Village (UV)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1109/UV50937.2020.9426189\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"2020 5th International Conference on Universal Village (UV)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/UV50937.2020.9426189","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
B-factor and Light-induced Allostery in NMDA Receptors
Light-sensitive protein with the light-induced allostery has great applications in bio-medical researches, which can be obtained by introducing the mutation at certain site in the protein. In the present work, we investigate the experimental data on NMDA receptors with light-sensitive mutations, and propose empirical formulas to connect the structural factors to the observable electric current change, which is the signature of the light-induced allosteric effect. We found our formulas present reasonable agreement with experimental data using the full-length structure of NMDA receptor 4tll. It can be used to predict the light-sensitive phenomena of this protein with other types of mutation. Present method can be directly extended to other proteins beyond the current 4tll.