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Author: Centonze, VE
Author: Firulli, AB
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Methods Article

Fluorescence Resonance Energy Transfer (FRET) as a method to calculate the dimerization strength of basic Helix-Loop-Helix (bHLH) proteins

Victoria E. Centonze1, Beth A. Firulli2 and Anthony B. Firulli2*

1 Department of Cellular and Structural Biology University of Texas Health Science Center at San Antonio. USA.
2 Wells Center for Pediatric Research, James Whitcomb Riley Hospital for Children, Departments of Pediatrics and Medical & Molecular Genetics, Indiana University Medical School. 1044 W. Walnut, R4 372, Indianapolis, IN. 46202-5225. USA.

* To whom correspondence should be addressed: Anthony B. Firulli, Wells Center for Pediatric Research, James Whitcomb Riley Hospital for Children, Departments of Pediatrics and Medical & Molecular Genetics, Indiana University Medical School. 1044 W. Walnut, R4 372, Indianapolis, IN. 46202-5225. USA. Email: tfirulli@iupui.edu

Biol. Proced. Online 2004;6:78-82. doi:10.1251/bpo75
Submitted: March 17, 2004; Accepted: May 03, 2004; Published: May 12, 2004.

Indexing terms: Phosphorylation; Fluorescence Resonance Energy Transfer; Transcription factors.


Figure 1 Enlarged

Fig. 1:

Representive images of FRET HAND1 homodimer experiment. HAND1YFP and HAND1T107;S109DCFP were cotransfected into HEK293 cells growing on coverslips as described, grown for 48 hr, fixed and mounted onto slides. Images prephotobleach show relative equal intensities of YFP and CFP emission. White arrow indicates the position of the cell which has been photobleached and + shows visually the increase on CFP emission. Note that the unbleached cell maintains consistent emission for both YFP and CFP.

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