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dc.contributor.authorAdams, Lauren
dc.contributor.authorAndrews, Ryan
dc.contributor.authorSchmit, Heidi
dc.contributor.authorBailey-Hartsel, Scott
dc.contributor.authorHati, Sanchita
dc.date.accessioned2016-10-14T16:51:49Z
dc.date.available2016-10-14T16:51:49Z
dc.date.issued2016-10-14T16:51:49Z
dc.identifier.urihttp://digital.library.wisc.edu/1793/75446
dc.descriptionColor poster with text, images, and graphs.en
dc.description.abstractMost computational and experimental studies to understand the molecular mechanism of an enzyme-catalyzed reaction are usually performed in dilute solutions. However, enzymatic activities in vivo occur in a crowded environment composed of many macromolecules. We are performing computational, spectroscopic, and kinetic studies to investigate the impact of macromolecular crowding on the structure and enzymatic activity of Escherichia coli prolyl-tRNA synthetase. This enzyme is a member of an important family of enzymes, which are essential for the biosynthesis of proteins in all living organisms. The overall goal is to evaluate if there is a need for consideration of the effect of macromolecular crowding for structure-based drug design to inhibit the function of pathogenic prolyl-tRNA synthetases.en
dc.description.sponsorshipUniversity of Wisconsin--Eau Claire Office of Research and Sponsored Programsen
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589;
dc.subjectprolyl-tRNA synthetaseen
dc.subjectEscherichia colien
dc.subjectMacromolecular crowdingen
dc.subjectPostersen
dc.titleSpectroscopic Studies to Explore the Impact of Macromolecular Crowding on the Structure and Function of Escherichia coli of Prolyl-tRNA Synthetaseen
dc.typePresentationen


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