Single-molecule mechanical response of no mechanoreceptor potential C channel studied with magnetic tweezer = 자기집게를 이용한 No Mechanoreceptor Potential C 의 역학적 반응에 대한 연구

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Touch sensing is essential to human communication, quality of life and health; however, the underlying molecular mechanisms remain mostly unknown. Touch is mediated by ion channels on sensory neurons, such as Transient receptor potential (TRP) channels. Recently drosophila’s mechanosensory TRP channel, No mechanoreceptor potential C (NOMPC) has been illuminated as a possible direct gating ion channel that transduces mechanical stimuli into electrical and chemical signals by opening its ion pore. Here, we first demonstrate features of NOMPC using total internal reflection fluorescence (TIRF) microscopy and magnetic tweezer. We showed the stable tetrameric formation by bleaching the eGFP-NOMPC recombinant protein with laser on TIRF microscopy. Also we pulled eGFP-NOMPC-Spytag recombinant protein using magnetic tweezer to discover the mechanical characteristics of NOMPC. Ours study established the preliminary experimental environments to understanding the unexplored mechanism of NOMPC.
Advisors
Cho, Yong-Hoonresearcher조용훈researcher
Description
한국과학기술원 :물리학과,
Publisher
한국과학기술원
Issue Date
2016
Identifier
325007
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 물리학과, 2016.8,[ii, 20 p. :]

Keywords

Magnetic tweezer▼amechanosensing ion channel▼aTIRF microscopy▼aNOMPC▼amembrane protein; 자기집게▼a역학적 이온통로▼a전반사현미경▼aNOMPC▼a막 단백질

URI
http://hdl.handle.net/10203/266101
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=849871&flag=dissertation
Appears in Collection
PH-Theses_Master(석사논문)
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