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. 1989 Aug;56(2):415–420. doi: 10.1016/S0006-3495(89)82687-6

Determination of the fractal dimension of membrane protein aggregates using fluorescence energy transfer.

T G Dewey 1, M M Datta 1
PMCID: PMC1280490  PMID: 2528385

Abstract

It is demonstrated that fluorescence resonance energy transfer may be used to determine the fractal dimension of aggregates of membrane-bound proteins. Theoretical and experimental results are presented for two different experimental designs: energy transfer between proteins and energy transfer from lipids to proteins. For energy transfer between proteins the lattice spacing must be known independently for a fractal dimension to be uniquely determined, and this represents a disadvantage to this experimental design. Results are presented for the calcium ATPase and a fractal dimension of 1.9 is estimated for ATPase aggregates by assuming a lattice spacing of 50 A. Energy transfer from lipids to protein provides a means of estimating the length of the "coast-line" of the aggregate. In this case the fractal dimension is uniquely determined from a log-log plot. An analysis of data for bacteriohodopsin reconstituted in phospholipid vesicles gives a fractal dimension of 1.6. The structural basis of the value for the fractal dimension is discussed for these two systems. These techniques provide a means of assessing the nature of protein-protein interactions in membranous systems.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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