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UV Thermal Melting Curves of tRNAPhe in the Presence of Ligands

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Sarah R. Kirk , Todd P. Silverstein and Karen L. McFarlane Holman

Department of Chemistry, Willamette University, Salem, OR 97301

J. Chem. Educ., 2008, 85 (5), p 674

DOI: 10.1021/ed085p674

Publication Date (Web): May 1, 2008

Abstract

This laboratory project is one component of a semester-long advanced biochemistry laboratory course that uses several complementary techniques to study tRNA^Phe conformational chvanges induced by ligand binding. In this article we describe a set of experiments in which the thermal unfolding of tRNA^Phe is studied with UV–vis spectrophotometry. Over the course of two laboratory periods, students examine the effects of magnesium and small molecule ligands on tRNA^Phe conformational stability. The data collected in this laboratory are fit to saturation binding curves, the ligand-binding equilibrium constants are determined, and conclusions are drawn about tRNA^Phe ligand binding modes and the impact of various types of ligands on tRNA structure.

Keywords (Audience):

Upper-Division Undergraduate

Keywords (Domain):

Biochemistry

Keywords (Pedagogy):

Hands-On Learning / Manipulatives

Keywords (Subject):

Bioinorganic Chemistry

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This article has been cited by 1 ACS Journal articles (1 most recent appear below).

Probing Changes in the Conformation of tRNAPhe: An Integrated Biochemistry Laboratory Course
Sarah R. Kirk , Todd P. Silverstein , Karen L. McFarlane Holman and Buck L. H. Taylor
Journal of Chemical Education2008 85 (5), 666
- Probing Changes in the Conformation of tRNAPhe: An Integrated Biochemistry Laboratory Course
  Sarah R. Kirk , Todd P. Silverstein , Karen L. McFarlane Holman and Buck L. H. Taylor
  Journal of Chemical Education2008 85 (5), 666
  We have designed a new guided-inquiry laboratory for an advanced biochemistry course. This integrated laboratory focuses on the biomolecule tRNAPhe and combines elements of bioorganic and bioinorganic chemistry with biochemistry. Throughout the semester ...
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