A new view of protein synthesis: mapping the free energy landscape of the ribosome using single-molecule FRET. Review uri icon

Overview

MeSH

  • Binding Sites
  • Computer Simulation
  • Mutagenesis, Site-Directed
  • RNA, Transfer

MeSH Major

  • Fluorescence Resonance Energy Transfer
  • Protein Biosynthesis
  • Ribosomes
  • Thermodynamics

abstract

  • This article reviews the application of single-molecule fluorescence resonance energy transfer (smFRET) methods to the study of protein synthesis catalyzed by the ribosome. smFRET is a powerful new technique that can be used to investigate dynamic processes within enzymes spanning many orders of magnitude. The application of wide-field smFRET imaging methods to the study of dynamic processes in the ribosome offers a new perspective on the mechanism of protein synthesis. Using this technique, the structural and kinetic parameters of tRNA motions within wild-type and specifically mutated ribosome complexes have been obtained that provide valuable new insights into the mechanism and regulation of translation elongation. The results of these studies are discussed in the context of current knowledge of the ribosome mechanism from both structural and biophysical perspectives.

publication date

  • July 2008

has subject area

  • Binding Sites
  • Computer Simulation
  • Fluorescence Resonance Energy Transfer
  • Mutagenesis, Site-Directed
  • Protein Biosynthesis
  • RNA, Transfer
  • Ribosomes
  • Thermodynamics

Research

keywords

  • Journal Article
  • Review

Identity

Language

  • eng

PubMed Central ID

  • PMC2930612

Digital Object Identifier (DOI)

  • 10.1002/bip.20961

PubMed ID

  • 18286627

Additional Document Info

start page

  • 565

end page

  • 577

volume

  • 89

number

  • 7