Exploring the Interplay of Dynamics and Catalysis in Escherichia coli Prolyl-tRNA Synthetase

dc.contributor.advisor	Hati, Sanchita
dc.contributor.advisor	Bhattacharyya, Sudeep
dc.contributor.author	Huynh, Tiffany
dc.contributor.author	Reinhardt, Clorice
dc.date.accessioned	2016-03-24T20:23:07Z
dc.date.available	2016-03-24T20:23:07Z
dc.date.issued	2015-04
dc.description	Color poster with text, models, graphs, and images.	en
dc.description.abstract	We are using quantum mechanical/molecular mechanical approaches to model and compute energetics of adenylate formation reaction in enzyme and enzyme-free system. Herein, we have presented the preliminary results of our study, which include the free-energy of activation of aminoacyl adenylate formation in aqueous solvent and the QM/MM-treated substrates-bound enzyme system.	en
dc.description.sponsorship	XSEDE Grant (CHE-110018); University of Wisconsin--Eau Claire Office of Research and Sponsored Programs	en
dc.identifier.uri	http://digital.library.wisc.edu/1793/74470
dc.language.iso	en_US	en
dc.relation.ispartofseries	USGZE AS589	en
dc.subject	Aminoacyl-tRNA synthetases	en
dc.subject	Escherichia coli	en
dc.subject	Prolyl-rRNA synthetases	en
dc.subject	Protein dynamics	en
dc.subject	Posters	en
dc.title	Exploring the Interplay of Dynamics and Catalysis in Escherichia coli Prolyl-tRNA Synthetase	en
dc.type	Presentation	en

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