Use of the A. Victoria Green Fluorescent Protein to Study Protein Dynamics In Vivo

Jason A. Kahana1, Pam A. Silver2

1 University of California, San Diego, California, 2 Dana‐Farber Cancer Institute, Boston, Massachusetts
Publication Name:  Current Protocols in Neuroscience
Unit Number:  Unit 5.15
DOI:  10.1002/0471142301.ns0515s14
Online Posting Date:  May, 2001
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Abstract

Fluorescent molecules serve as valuable tools for the detection of numerous biochemical phenomena and have been employed for protein localization, quantitation of gene expression, detection of nucleic acids, cell sorting and determination of chemical concentrations. However, the use of such techniques generally requires significant nonphysiological perturbations to the biological system being studied; therefore, they are not always appropriate for the observation of dynamic phenomena. Green fluorescent protein (GFP), cloned from jellyfish, has been used to overcome many of these problems. It is a small, extremely stable fluorescent protein that has been successfully expressed and detected in a wide variety of organisms, both in intact form and fused to other proteins. This overview unit describes the use of this proteinaceous fluorophore for in vivo observation of cellular phenomena.

     
 
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Table of Contents

  • Overview of GFP Fluorescence
  • Utilization of GFP
  • Problems with GFP
  • Mutants of GFP
  • Literature Cited
  • Figures
     
 
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Materials

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Figures

Videos

Literature Cited

Literature Cited
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