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dc.contributor.advisorBhattacharyay, Sudeep
dc.contributor.advisorHati, Sanchita
dc.contributor.authorFehling, Samuel
dc.contributor.authorStrom, Alexander M.
dc.date.accessioned2014-10-02T16:07:35Z
dc.date.available2014-10-02T16:07:35Z
dc.date.issued2014-04
dc.identifier.urihttp://digital.library.wisc.edu/1793/69794
dc.descriptionColor poster with text, images, and graphs.en
dc.description.abstractAminoacyl-tRNA synthetases (AARSs) catalyze the esterification of transfer RNAs with their cognate amino acids. These multi-domain enzymes undergo conformational changes upon substrate binding. To understand the molecular mechanism of the population-shift from substrate-free conformations to bound conformation(s), the purpose of this study was to analyze the substrate-bound and substrate-free conformations of E. Faecalis Prolyl-tRNA Synthetase (ProRS) by performing Principal Component Analysis (PCA) of the molecular dynamic simulation trajectories.en
dc.description.sponsorshipUniversity of Wisconsin--Eau Claire Office of Research and Sponsored Programs.en
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589en
dc.subjectAminocycl-tRNA Synthetasesen
dc.subjectSubstrate bindingen
dc.subjectE. Faecalis prolyl-tRNA Synthetase (ProRS)en
dc.subjectPostersen
dc.titlePrincipal Component Analysis to Explore Transition Pathway of the Conformational Change in E. Faecalis Prolyl-tRNA Synthetase upon Substrate Bindingen
dc.typePresentationen


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