TY - JOUR
T1 - Distance Parameters Derived from Time-Resolved Förster Resonance Energy Transfer Measurements and Their Use in Structural Interpretations of Thermodynamic Quantities Associated with Protein-DNA Interactions
AU - Parkhurst, Lawrence J.
N1 - Funding Information:
I thank Mr. Roberto Fabio Delgadillo for Fig. 6 , and acknowledge support from NIH Grants GM 59346, CA 76049, and RR 15635.
PY - 2004
Y1 - 2004
N2 - Parameters that characterize a distance distribution P(R) can be obtained from time-resolved FRET measurements. These measurements can involve various combinations of donor-detected FRET and acceptor-detected FRET constrained by steady state emission intensity differences between the donor and that of the donor in the presence of an acceptor. Highly precise average interdye distances R can ultimately lead to precise intramolecular distances in solution. The width of the P(R) distribution, δ, preferably and more precisely after removal of the tether contributions, yields a measure of conformational equilibria and of conformational dynamics of the macromolecule to which the probes are attached. FRET measurements combined with equilibrium determinations and with rapid-mixing or relaxation kinetics provide structure-energy, entropy profiles of intermediates and transition states along the reaction coordinate.
AB - Parameters that characterize a distance distribution P(R) can be obtained from time-resolved FRET measurements. These measurements can involve various combinations of donor-detected FRET and acceptor-detected FRET constrained by steady state emission intensity differences between the donor and that of the donor in the presence of an acceptor. Highly precise average interdye distances R can ultimately lead to precise intramolecular distances in solution. The width of the P(R) distribution, δ, preferably and more precisely after removal of the tether contributions, yields a measure of conformational equilibria and of conformational dynamics of the macromolecule to which the probes are attached. FRET measurements combined with equilibrium determinations and with rapid-mixing or relaxation kinetics provide structure-energy, entropy profiles of intermediates and transition states along the reaction coordinate.
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U2 - 10.1016/S0076-6879(04)79013-8
DO - 10.1016/S0076-6879(04)79013-8
M3 - Article
C2 - 15051361
AN - SCOPUS:1542358918
SN - 0076-6879
VL - 379
SP - 235
EP - 262
JO - Methods in enzymology
JF - Methods in enzymology
ER -