Repository logo
  • English
  • 中文
Log In
Have you forgotten your password?
  1. Home
  2. College of Engineering / 工學院
  3. Engineering Science and Ocean Engineering / 工程科學及海洋工程學系
  4. Prediction of Transcription Factor Domain based on Analysis of Specific and non-Specific DNA-Binding Residues on the Protein Sequence
 
  • Details

Prediction of Transcription Factor Domain based on Analysis of Specific and non-Specific DNA-Binding Residues on the Protein Sequence

Date Issued
2009
Date
2009
Author(s)
Huang, Chun-Chin
URI
http://ntur.lib.ntu.edu.tw//handle/246246/188998
Abstract
Protein-DNA interactions are essential for fundamental biochemical activities including DNA transcription, replication, packaging, repair and rearrangement. Proteins interacting with DNA can be classified into two modes distinguished by sequence-specific and non-specific binding respectively. Protein-DNA specific binding provides a mechanism to recognize correct nucleotide base pairs namely sequence-specific identification. On the other hand, protein-DNA non-specific binding shows relatively little base-sequence preference and interacts with DNA backbone.n this thesis, we present a two stage Protein-DNA binding prediction. In the first stage of DNA-binding residues prediction, the predictor for DNA specific binding residues achieves 96.45% accuracy with 50.14% sensitivity, 99.31% specificity, 81.70% precision, and 62.15% F-measure. The predictor for DNA non-specific binding residues achieves 89.14% accuracy with 53.06% sensitivity, 95.25% specificity, 65.47% precision, and 58.62% F-measure. In addition, we combine the results of sequence-specific and non-specific binding residues predicted in previous stage with OR operation, and the predictor achieves 89.26% accuracy with 56.86% sensitivity, 95.63% specificity, 71.92% precision, and 63.51% F-measure. In the second stage, a protein-DNA interaction mode predictor is proposed. It can achieve 75.83% accuracy while using support vector machine with multi-class prediction.his article presents the design of a sequence-based predictor aiming to identify the sequence-specific and non-specific DNA-binding residues in a transcription factor with DNA binding-mechanism concerned. The protein-DNA interaction mode prediction was introduced to provide biochemist more structural hint and help improve previous DNA-binding residues prediction. In addition, we will exploit the experiences learned in this study to design binding-mechanism concerned predictors for other types of DNA-contacted proteins.
Subjects
DNA-binding residues prediction
sequence-specific binding
non-specific binding
support vector machine
transcription factor
Type
thesis
File(s)
Loading...
Thumbnail Image
Name

ntu-98-R96525072-1.pdf

Size

23.53 KB

Format

Adobe PDF

Checksum

(MD5):65cb17af6afe5f140da204d2ceb17032

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