Domain-Domain Communication for tRNA Aminoacylation : Importance of Evolutionarily Conserved and Energetically Coupled Residues.

dc.contributor.advisor	Hati, Sanchita
dc.contributor.author	Weimer, Kristina
dc.contributor.author	Shane, Brianne
dc.date.accessioned	2009-02-10T18:29:39Z
dc.date.available	2009-02-10T18:29:39Z
dc.date.issued	2009-02-10T18:29:39Z
dc.description	Color poster with text and images describing research conducted by Brianne Shane and Kristina Weimer, advised by Sanchita Hati.	en
dc.description.abstract	Aminoacyl tRNA synthetases (ARSs) are an important family of protein enzymes that play a key role in protein biosynthesis. ARSs catalyze the covalent attachment of amino acids to their cognate transfer RNA (tRNA). In the present work, we investigated the molecular basis of long-range domain-domain communication in Escherichia coliprolyl-tRNA synthetase (E. coli ProRS).	en
dc.description.sponsorship	University of Wisconsin--Eau Claire Office of Research and Sponsored programs.	en
dc.identifier.uri	http://digital.library.wisc.edu/1793/32224
dc.language.iso	en_US	en
dc.relation.ispartofseries	USGZE AS589	en
dc.subject	RNA	en
dc.subject	Aminocyl-tRNA synthetases	en
dc.subject	RNA-protein interactions	en
dc.subject	Proteins--Synthesis	en
dc.subject	Posters	en
dc.title	Domain-Domain Communication for tRNA Aminoacylation : Importance of Evolutionarily Conserved and Energetically Coupled Residues.	en
dc.type	Presentation	en

Files

Now showing 1 - 2 of 2

Now showing 1 - 1 of 1