Exploring the Role of Distant Domain Dynamics in Substrate Binding of Escherichia Coli Prolyl-tRNA Synthetase

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dc.contributor.advisorHati, Sanchita
dc.contributor.advisorBhattacharyay, Sudeep
dc.contributor.authorMocol, Matthew
dc.date.accessioned2016-04-08T13:47:35Z
dc.date.available2016-04-08T13:47:35Z
dc.date.issued2015-04
dc.descriptionColor poster with text, graphs, and images.en
dc.description.abstractOur results demonstrate that the presence of the INS is critical to provide the required energy barrier for the substrate to be bound to the catalytic core, instead of getting spontaneously hydrolyzed.en
dc.description.sponsorshipUniversity of Wisconsin--Eau Claire Office of Research and Sponsored Programsen
dc.identifier.urihttp://digital.library.wisc.edu/1793/74664
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589en
dc.subjectInsertion domain (INS)en
dc.subjectChemistryen
dc.subjectProlyl-tRNA synthetaseen
dc.subjectEscherichia colien
dc.subjectPostersen
dc.titleExploring the Role of Distant Domain Dynamics in Substrate Binding of Escherichia Coli Prolyl-tRNA Synthetaseen
dc.typePresentationen

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