Show simple item record

dc.contributor.advisorHati, Sanchita
dc.contributor.advisorBhattacharyay, Sudeep
dc.contributor.authorWeimer, Kristina
dc.contributor.authorShane, Brianne
dc.contributor.authorBrunetto, Michael
dc.date.accessioned2009-02-11T20:02:25Z
dc.date.available2009-02-11T20:02:25Z
dc.date.issued2009-02-11T20:02:25Z
dc.identifier.urihttp://digital.library.wisc.edu/1793/32284
dc.descriptionColor poster with text and disgrams describing research conducted by Kristina Weimer, Brianne Shane, and Michael Brunetto, advised by Sudeep Bhattacharyay and Sanchita Hati.en
dc.description.abstractLeucyl-tRNA synthetases are class I synthetases that catalyze the covalent attachment of leucine to the tRNAL. The three-dimensional crystal structure of Thermus thermophilus leucyl-tRNA synthetase (TtLeuRS) demonstrates a complex modular architecture where three flexible domains [the conserved connective polypeptide 1 (CP1) domain (residues 224-417), the leucine-specific (LS) domain (residues 577-634), and the zinc-1 (ZN-1) binding domain (residues 154-189)] are inserted into the central catalytic domain. In the present work, we have investigated the collective motion of various structural elements in TtLeuRS using normal mode calculations.en
dc.description.sponsorshipUniversity of Wisconsin--Eau Claire Office of Research and Sponsored Programs.en
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589en
dc.subjectRNAen
dc.subjectAminoacyl-tRNA synthetaseen
dc.subjectLeucineen
dc.subjectAmino acidsen
dc.subjectPostersen
dc.titleExploring Cooperative Domain Dynamics in Thermus thermophilus Leucyl-tRNA Synthetase Using Low-Frequency Normal Mode Calculations and Statistical Coupling Analysis.en
dc.typePresentationen


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

  • Student Research Day
    Posters of collaborative student/faculty research presented at Student Research Day

Show simple item record