Repository logo
  • English
  • 中文
Log In
Have you forgotten your password?
  1. Home
  2. College of Science / 理學院
  3. Chemistry / 化學系
  4. Label-Free Detections of GST-fused Protein and the Interaction of Proteins via Silicon Nanowire Field-Effect Transistor
 
  • Details

Label-Free Detections of GST-fused Protein and the Interaction of Proteins via Silicon Nanowire Field-Effect Transistor

Date Issued
2010
Date
2010
Author(s)
Yang, Jia-Xun
URI
http://ntur.lib.ntu.edu.tw//handle/246246/257395
Abstract
Nanosensors have been developed for recent several years, and have potential on sensing charged molecules because the properties of high-sensitivity and label-free. This thesis is about sensing the protein-protein interactions via silicon nanowire field-effect transistor. Proteins often participate in the machanisms for the maintaining of physiology in cells with such interactions. If the detections of the interactions which is not confirmed could be rapid and quantitative, that will be much helpful to realize the functions of the proteins and the realative treatments of diseases caused from the abnormal functions of proteins. By the immobilization of proteins to the surface of the silicon nanowires, the conductance of nanowires will be affected by the electric field of the charged proteins.And we could observe the changes of the conductance caused by the association of proteins and comfirm the interaction between proteins. About calmodulin, the association of troponin I and calmodulin had been detected succefully in specific range of calcium concentration. Furthermore, we detected the association of N-type voltage-gated calcium channel and calmodulin in physiological condition. That proves the possibility and advantages of the silicon nanowire field-effect transistor as a biosensor. About Rab3A, we observed the dissociation of GDP and Rab3A in pure phosphate buffer solution. The reversible association-dissociation of GDP and Rab3A illustrates that dissociation rate should be taked in consideration in experiments about Rab3A activated by GTP. With the advantages of GST pull-dwon assay, we have developed a reusable, label-free and high sensitivity biosensor chip which could detect the protein-protein interactions in physiological conditions, provides us to understand the function of the proteins.
Subjects
silicon nanowire field-effect transistor
calmodulin
calcium ion
glutathione-S-transferase
N-type voltage-gated calcium channel
Rab3A
GDP
Type
thesis
File(s)
Loading...
Thumbnail Image
Name

ntu-99-R97223169-1.pdf

Size

23.32 KB

Format

Adobe PDF

Checksum

(MD5):5826f8529853f106e0853d1f462bb834

臺大位居世界頂尖大學之列,為永久珍藏及向國際展現本校豐碩的研究成果及學術能量,圖書館整合機構典藏(NTUR)與學術庫(AH)不同功能平台,成為臺大學術典藏NTU scholars。期能整合研究能量、促進交流合作、保存學術產出、推廣研究成果。

To permanently archive and promote researcher profiles and scholarly works, Library integrates the services of “NTU Repository” with “Academic Hub” to form NTU Scholars.

總館學科館員 (Main Library)
醫學圖書館學科館員 (Medical Library)
社會科學院辜振甫紀念圖書館學科館員 (Social Sciences Library)

開放取用是從使用者角度提升資訊取用性的社會運動,應用在學術研究上是透過將研究著作公開供使用者自由取閱,以促進學術傳播及因應期刊訂購費用逐年攀升。同時可加速研究發展、提升研究影響力,NTU Scholars即為本校的開放取用典藏(OA Archive)平台。(點選深入了解OA)

  • 請確認所上傳的全文是原創的內容,若該文件包含部分內容的版權非匯入者所有,或由第三方贊助與合作完成,請確認該版權所有者及第三方同意提供此授權。
    Please represent that the submission is your original work, and that you have the right to grant the rights to upload.
  • 若欲上傳已出版的全文電子檔,可使用Open policy finder網站查詢,以確認出版單位之版權政策。
    Please use Open policy finder to find a summary of permissions that are normally given as part of each publisher's copyright transfer agreement.
  • 網站簡介 (Quickstart Guide)
  • 使用手冊 (Instruction Manual)
  • 線上預約服務 (Booking Service)
  • 方案一:臺灣大學計算機中心帳號登入
    (With C&INC Email Account)
  • 方案二:ORCID帳號登入 (With ORCID)
  • 方案一:定期更新ORCID者,以ID匯入 (Search for identifier (ORCID))
  • 方案二:自行建檔 (Default mode Submission)
  • 方案三:學科館員協助匯入 (Email worklist to subject librarians)

Built with DSpace-CRIS software - Extension maintained and optimized by 4Science