Simultaneous determination of intramolecular distance distributions and conformational dynamics by global analysis of energy transfer measurements

J. M. Beechem; E. Haas

doi:10.1016/S0006-3495(89)82918-2

Simultaneous determination of intramolecular distance distributions and conformational dynamics by global analysis of energy transfer measurements

J. M. Beechem, E. Haas

University of Illinois at Urbana-Champaign

Research output: Contribution to journal › Article › peer-review

147 Scopus citations

Abstract

Fluorescence energy transfer is widely used for determination of intramolecular distances in macromolecules. The time dependence of the rate of energy transfer is a function of the donor/acceptor distance distribution and fluctuations between the various conformations which may occur during the lifetime of the excited state. Previous attempts to recover both distance distributions and segmental diffusion from time-resolved experiments have been unsuccessful due to the extreme correlation between fitting parameters. A method has been developed, based on global analysis of both donor and acceptor fluorescence decay curves, which overcomes this extreme cross-correlation and allows the parameters of the equilibrium distance distributions and intramolecular diffusion constants to be recovered with high statistical significance and accuracy. Simulation studies of typical intramolecular energy transfer experiments reveal that both static and dynamic conformational distribution information can thus be obtained at a single temperature and viscosity.

Original language	English
Pages (from-to)	1225-1236
Number of pages	12
Journal	Biophysical Journal
Volume	55
Issue number	6
DOIs	https://doi.org/10.1016/S0006-3495(89)82918-2
State	Published - Jun 1989
Externally published	Yes

Bibliographical note

Funding Information:
port of the National Institutes of Health General Medical Sciences (NIH grants R01-GM39372-01 and RO1-GM41360-01) and the United States-Israel Bi-national Science Grant Foundation (grant 217/84).

Funding Information:
J. M. Beechem gratefully acknowledges support from the Lucille P. Markey Foundation. J. M. Beechem is a Lucille P. Markey Scholar in Biomedical Sciences. The Laboratory for Fluorescence Dynamics (LFD) is supported jointly by the Division of Research Resources of the National Institutes of Health (RRO3155-01) and the University of Illinois Urbana-Champaign. E. Haas gratefully acknowledges the sup-

Funding

port of the National Institutes of Health General Medical Sciences (NIH grants R01-GM39372-01 and RO1-GM41360-01) and the United States-Israel Bi-national Science Grant Foundation (grant 217/84). J. M. Beechem gratefully acknowledges support from the Lucille P. Markey Foundation. J. M. Beechem is a Lucille P. Markey Scholar in Biomedical Sciences. The Laboratory for Fluorescence Dynamics (LFD) is supported jointly by the Division of Research Resources of the National Institutes of Health (RRO3155-01) and the University of Illinois Urbana-Champaign. E. Haas gratefully acknowledges the sup-

Funders	Funder number
National Institute of General Medical Sciences	R01GM039372

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10.1016/S0006-3495(89)82918-2

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title = "Simultaneous determination of intramolecular distance distributions and conformational dynamics by global analysis of energy transfer measurements",

abstract = "Fluorescence energy transfer is widely used for determination of intramolecular distances in macromolecules. The time dependence of the rate of energy transfer is a function of the donor/acceptor distance distribution and fluctuations between the various conformations which may occur during the lifetime of the excited state. Previous attempts to recover both distance distributions and segmental diffusion from time-resolved experiments have been unsuccessful due to the extreme correlation between fitting parameters. A method has been developed, based on global analysis of both donor and acceptor fluorescence decay curves, which overcomes this extreme cross-correlation and allows the parameters of the equilibrium distance distributions and intramolecular diffusion constants to be recovered with high statistical significance and accuracy. Simulation studies of typical intramolecular energy transfer experiments reveal that both static and dynamic conformational distribution information can thus be obtained at a single temperature and viscosity.",

author = "Beechem, {J. M.} and E. Haas",

note = "Funding Information: port of the National Institutes of Health General Medical Sciences (NIH grants R01-GM39372-01 and RO1-GM41360-01) and the United States-Israel Bi-national Science Grant Foundation (grant 217/84). Funding Information: J. M. Beechem gratefully acknowledges support from the Lucille P. Markey Foundation. J. M. Beechem is a Lucille P. Markey Scholar in Biomedical Sciences. The Laboratory for Fluorescence Dynamics (LFD) is supported jointly by the Division of Research Resources of the National Institutes of Health (RRO3155-01) and the University of Illinois Urbana-Champaign. E. Haas gratefully acknowledges the sup-",

year = "1989",

month = jun,

doi = "10.1016/S0006-3495(89)82918-2",

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AB - Fluorescence energy transfer is widely used for determination of intramolecular distances in macromolecules. The time dependence of the rate of energy transfer is a function of the donor/acceptor distance distribution and fluctuations between the various conformations which may occur during the lifetime of the excited state. Previous attempts to recover both distance distributions and segmental diffusion from time-resolved experiments have been unsuccessful due to the extreme correlation between fitting parameters. A method has been developed, based on global analysis of both donor and acceptor fluorescence decay curves, which overcomes this extreme cross-correlation and allows the parameters of the equilibrium distance distributions and intramolecular diffusion constants to be recovered with high statistical significance and accuracy. Simulation studies of typical intramolecular energy transfer experiments reveal that both static and dynamic conformational distribution information can thus be obtained at a single temperature and viscosity.

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Simultaneous determination of intramolecular distance distributions and conformational dynamics by global analysis of energy transfer measurements

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