View Item 
      •   Home
      • 1. Schools
      • College of Science
      • School of Biological Sciences (SBS)
      • SBS Theses (Open Access)
      • View Item
      •   Home
      • 1. Schools
      • College of Science
      • School of Biological Sciences (SBS)
      • SBS Theses (Open Access)
      • View Item
      JavaScript is disabled for your browser. Some features of this site may not work without it.
      Subject Lookup

      Browse

      All of DR-NTUCommunities & CollectionsTitlesAuthorsBy DateSubjectsThis CollectionTitlesAuthorsBy DateSubjects

      My Account

      Login

      Statistics

      Most Popular ItemsStatistics by CountryMost Popular Authors

      About DR-NTU

      NMR study of eukaryotic translation termination.

      Thumbnail
      PhD Thesis (10.47Mb)
      Author
      Wong, Leo E.
      Date of Issue
      2013
      School
      School of Biological Sciences
      Abstract
      Translation termination is critical. Many diseases are caused by nonsense mutation. Hence, understanding termination could pave the way to strategic interference of the process with medical benefit. Unlike in bacteria, eukaryotic translation termination is more complex. Exact mechanism of stop codon recognition by class I release factor eRF1 and the cooperative role of class II release factor eRF3 remain obscure. By solving the solution structures of both wild-type N-domain of human eRF1 exhibiting omnipotent specificity and its mutant with UGA-unipotency, we found the conserved GTS loop adopting alternate conformations. We propose that structural variability in the GTS loop may underline the switching between omnipotency and unipotency of eRF1. In addition, we showed the specific binding of a 15-mer RNA oligonucleotide mimicking the decoding region of 18S rRNA helix 44 to helix α1 of N-domain, on the interface that is shielded partially by C-domain in full-length eRF1. The 15-mer RNA displaces C-domain from the non-covalent NC-complex, suggesting an imperative domain rearrangement in eRF1 during which N-domain accommodates itself into ribosomal A site. On another hand, we also demonstrated the feasibility of targeted acquisition of NMR data that is dynamically controlled by the completeness of automatic backbone resonances assignment, in an effort to accelerate structural study of biomolecules by NMR spectroscopy.
      Subject
      DRNTU::Science::Biological sciences::Biochemistry
      Type
      Thesis
      Collections
      • SBS Theses (Open Access)

      Show full item record


      NTU Library, Nanyang Avenue, Singapore 639798 © 2011 Nanyang Technological University. All rights reserved.
      DSpace software copyright © 2002-2015  DuraSpace
      Contact Us | Send Feedback
      Share |    
      Theme by 
      Atmire NV
       

       


      NTU Library, Nanyang Avenue, Singapore 639798 © 2011 Nanyang Technological University. All rights reserved.
      DSpace software copyright © 2002-2015  DuraSpace
      Contact Us | Send Feedback
      Share |    
      Theme by 
      Atmire NV
       

       

      DCSIMG