Study on Bacterial Protein Synthesis System toward the Incorporation of D-Amino Acid & Synthesis of 2'-deoxy-3'-mercapto-tRNA

DSpace/Manakin Repository

Study on Bacterial Protein Synthesis System toward the Incorporation of D-Amino Acid & Synthesis of 2'-deoxy-3'-mercapto-tRNA

Citable link to this page

 

 
Title: Study on Bacterial Protein Synthesis System toward the Incorporation of D-Amino Acid & Synthesis of 2'-deoxy-3'-mercapto-tRNA
Author: Huang, Po-Yi
Citation: Huang, Po-Yi. 2014. Study on Bacterial Protein Synthesis System toward the Incorporation of D-Amino Acid & Synthesis of 2'-deoxy-3'-mercapto-tRNA. Doctoral dissertation, Harvard University.
Full Text & Related Files:
Abstract: Life is anti-entropic and highly organized phenomenon with two characteristics reinforcing each other: homochirality and the stereospecific catalysis of chemical reactions. The exclusive presence of L-amino acids and R-sugars in living world well depict this. Hypothetically, the amino acids and sugars of reverse chirality could form a parallel kingdom which is highly orthogonal to the present world. The components from this mirror kingdom, such as protein or nucleic acid, will be much more resistant to the defensive mechanism of present living system, which could be of great value. Therefore, by gradually rewiring the present bio-machineries, we look to build a bridge leading us to the space of mirror-imaged biomolecules. We begin by investigating protein synthesis with mirror amino acid since most amino acids contain one chiral center to be inversed comparing to sugars. In this work, we analyzed three stages critical for the incorporation of D-amino acid into ribosomal protein synthesis: amino acylation, EF-Tu binding of amino acyl-tRNA and delivery bias, and ribosome catalyzed peptidyl transfer. We have demonstrated that the affinity between EF-Tu and amino acyl-tRNA plays critical role on D-amino acid incorporation, and built a platform aimed to select for ribosome tolerating D-amino acid better.
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:12274132
Downloads of this work:

Show full Dublin Core record

This item appears in the following Collection(s)

 
 

Search DASH


Advanced Search
 
 

Submitters