Ensemble FRET methods in studies of intrinsically disordered proteins

Elisha Haas

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

20 Scopus citations


The main structural characteristic of intrinsically disordered proteins (IDPs) or intrinsically disordered regions of globular proteins is that they exist as ensembles of multiple conformers which can continuously interconvert, and at times, form ensembles of a more restricted number of conformers. Characterization of the disordered state and transitions to partially or fully ordered states of such ensembles must be expressed in statistical terms, i.e., determination of probability distributions of the various conformers. This can be achieved by measurements of time-resolved dynamic non-radiative excitation energy transfer within ensembles of site-specifically labeled IDP molecules. Distributions of intramolecular segmental end-to-end distances and their fast fluctuations can be determined and fast and slow conformational transitions within selected sections of the molecule can be monitored and analyzed.

Original languageEnglish
Title of host publicationIntrinsically Disordered Protein Analysis
Subtitle of host publicationVolume 1, Methods and Experimental Tools
EditorsVladimir Uversky, Vladimir Uversky, Keith Dunker
Number of pages32
StatePublished - 2012

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Distance distributions
  • Fast fluctuations and conformational transitions
  • IDP
  • Intramolecular diffusion coefficient
  • Site-specific labeling
  • Time resolved FRET


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