https://scholar.dgist.ac.kr/handle/20.500.11750/1177 2026-04-04T12:10:41Z https://scholar.dgist.ac.kr/handle/20.500.11750/57235 Title: Monitoring Rotation Dynamics of Membrane Protein in Live Cells Author(s): Park, Youngchan; Shin, Sangwon; Jin, Hyeonggyu; Park, Jiseong; Hong, Yeonki; Song, Hyunjoon; Seo, Daeha Abstract: Dynamic behavior of membrane protein provides critical information in molecular and cellular mechanisms. To have access to the mobility of a membrane protein, single-particle tracking has been advanced for the microscopic mechanism understandings. Among various molecular motions, however, only the lateral motion of the protein has been monitored due to the lack of in situ imaging tool enabling observation for rotation and vibration. Here, we developed plasmonic nanoparticles which can monitor rotational diffusion dynamics as well as lateral motion. This nanoparticle probe allows direct evidence and quantitative analysis of rotation dynamics, and furthermore, observation of conformation changes of proteins and the protein-protein interactions in live cells. This study provides an insight into the molecular mechanism regarding the intracellular signaling process. 2019-03-02T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/57233 Title: Analysis of Ion Channel Dynamics by Single Molecule Tracking in Live Cells Author(s): Hong, Yeonki; Park, Jiseong; Seo, Daeha Abstract: Protein dynamics play an important role in signal transduction in association with their activation mechanisms, functions, and so on. Single molecule tracking technique have been widely used for investigating diffusion behavior of protein in live cells. Especially membrane proteins have been studied since they are important to understand cell responding to the surroundings. However, not many ion channel proteins such as AMPAR, NMDAR, etc., have been monitored due to their complex system. Here, we observed ionotropic glutamate receptor in neuroblastoma SH-SY5Y cell using single-molecule imaging. The diffusion coefficient of the receptor was significantly low because the receptor has four subunits (tetramers) and each subunit possesses a four transmembrane domain. Furthermore, we also analyzed interaction between subunits using single molecule tracking, further investigation of the protein dynamics of the membrane proteins such as ionotropic receptors, their structure and protein activation mechanism will be possible. 2019-03-03T15:00:00Z