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Author(s)

Weimer, Kristina; Shane, Brianne; Brunetto, Michael

Advisor(s)

Hati, Sanchita; Bhattacharyay, Sudeep

Date

Feb 11, 2009

Subject(s)

RNA; Aminoacyl-tRNA synthetase; Leucine; Amino acids; Posters

Series

USGZE AS589

Abstract

Leucyl-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.

Description

Color poster with text and disgrams describing research conducted by Kristina Weimer, Brianne Shane, and Michael Brunetto, advised by Sudeep Bhattacharyay and Sanchita Hati.

Sponsor(s)

University of Wisconsin--Eau Claire Office of Research and Sponsored Programs.

Permanent link

http://digital.library.wisc.edu/1793/32284 

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Part of

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

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