Intramolecular three-colour single pair FRET of intrinsically disordered proteins with increased dynamic range

Mol Biosyst. 2012 Oct;8(10):2531-4. doi: 10.1039/c2mb25135c.

Abstract

Single molecule observation of fluorescence resonance energy transfer can be used to provide insight into the structure and dynamics of proteins. Using a straightforward triple-colour labelling strategy, we present a measurement and analysis scheme that can simultaneously study multiple regions within single intrinsically disordered proteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbocyanines
  • Color
  • Escherichia coli / genetics
  • Fluorescence Resonance Energy Transfer
  • Fluorescent Dyes
  • Humans
  • Hydrazines
  • Molecular Imaging / methods*
  • Nuclear Pore Complex Proteins / chemistry*
  • Nuclear Pore Complex Proteins / genetics
  • Organic Chemicals
  • Protein Conformation
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Spectrometry, Fluorescence
  • Staining and Labeling / methods*

Substances

  • Alexa 488 hydrazide
  • Alexa Fluor 647
  • Alexa594
  • Carbocyanines
  • Fluorescent Dyes
  • Hydrazines
  • NUP49 protein, S cerevisiae
  • Nuclear Pore Complex Proteins
  • Organic Chemicals
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins