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I'm a bit lost by this.  As you say, donor lifetime reduction caused by FRET is independent of concentration (so long as there is no external constraint on dimer formation), but since dimer formation is typically what brings the FRET partners into close proximity, I cannot see how you can expect to have increased FRET efficiency with less dimerization.  I may have misunderstood your point - if so, please clarify.  My brain is probably slowing down with age!

                               Guy

Optical Imaging Techniques in Cell Biology
by Guy Cox    CRC Press / Taylor & Francis
     http://www.guycox.com/optical.htm
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Associate Professor Guy Cox, MA, DPhil(Oxon) 
Australian Centre for Microscopy & Microanalysis, 
Madsen Building F09, University of Sydney, NSW 2006 

Phone +61 2 9351 3176     Fax +61 2 9351 7682
             Mobile 0413 281 861
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-----Original Message-----
From: Confocal Microscopy List [mailto:[log in to unmask]] On Behalf Of Straatman, Kees R. (Dr.)
Sent: Thursday, 17 November 2011 9:34 PM
To: [log in to unmask]
Subject: FRET-FLIM question

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Dear list members,

We have a discussion about FRET-FLIM at the moment and somebody has published that they see an increase in FRET efficiency and argues that this is because there is more dimerisation between the two proteins they are interested in. Now, I thought that FRET-FLIM is independent from the concentration of the fluorochromes and that the increase in FRET efficiency is caused by a change in distance between the 2 reporter FP (CFP and YFP) and it would be possible to have less dimerisation of the proteins but an increase in FRET efficiency. Is this correct?

Thanks

Kees

Dr Ir K.R. Straatman
Senior Experimental Officer
Centre for Core Biotechnology Services
College of Medicine, Biological Sciences and Psychology 
University of Leicester

http://www.le.ac.uk/biochem/microscopy/home.html

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