Structural interpretation of fluorescence resonanceenergy transfer measurements
Muscle Research Unit, Department of Anatomy. The University of Sydney NSW 2006, Australia
Fluorescence resonance energy transfer (FRET) has been widely used to determine distance information in macromolecular systems. However, little has been written about methods for combining FRET distances into coherent structural models. I argue that the methods used so far are inappropriate. This paper describes an algorithm specifically tailored for finding structures from FRET measurements. This algorithm finds structures which fit the experimentally measured parameter, the efficiency of energy transfer, rather than derived distances. The algorithm was implemented in Mathematica and applied to FRET distances obtained for the contractile protein actin. The approach used is applicable to other experimental techniques which measure distances between a relatively small number of loci.
Received on November 17, 1990; accepted on March 20, 1991
This article has been cited by other articles:
![]() |
S. K. Van Why, A. S. Mann, T. Ardito, G. Thulin, S. Ferris, M. A. Macleod, M. Kashgarian, and N. J. Siegel Hsp27 Associates with Actin and Limits Injury in Energy Depleted Renal Epithelia J. Am. Soc. Nephrol., January 1, 2003; 14(1): 98 - 106. [Abstract] [Full Text] [PDF] |
||||
