Hiring in life sciences? Share your open positions with our professional community. Read more Close

Advertisement

Fluorescence resonance energy transfer (FRET) as a method to calculate the dimerization strength of basic Helix-Loop-Helix (bHLH) proteins

External protocol Created on 10 Apr 2014

Authors

Victoria E. Centonze, Beth A. Firulli, Anthony B. Firulli

Summary

Post-translational modifications such as phosphorylation play a vital role in the regulation of protein function. In our study of the basic Helix-loop-Helix (bHLH) transcription factor HAND1, we show that HAND1 is phosphorylated during the trophoblast giant cell differentiation on residues residing in Helix I of the bHLH domain. Our hypothesis is that these modifications result in changes in HAND1 dimerization affinities with other bHLH factors. To test this idea, we employed FRET to measure the protein-protein interactions of HAND1 and HAND1 point mutants in HEK293 cells using YFP and CFP fusion proteins and laser scanning confocal microscopy.

Further details

The protocol was imported from Springer Protocols. To see the entire protocol, click on the source link, or download the pdf here.

Advertisement

Stats

  • Recommendations n/a n/a positive of 0 vote(s)
  • Views 272
  • Comments 0

Recommended by

  • No recommendations yet.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.

Advertisement