Table

Table 1. Physiological indicators using fluorescence resonance energy transfer

Wavelength (nm)a Maximum emission ratio changeb
Analyte or process Donor and acceptorc ΔFRETd Donor excitation Donor emission Acceptor emission References
Depolarization Coumarin-phosphatidylethanolamine; bis(thio barbiturate)trimethineoxonol 414 450 560 1.8/(100 mV) Gonzalez and Tsien (1997)
cAMP PKA catalytic subunit-FITC; PKA regulatory subunit-TROSue 495 520 580 1.6-2.2 Adams et al. (1991, 1993)
Trypsin BFP-(trypsin-sensitive linker)-GFP 380 445 507 4.6 Heim and Tsien (1996)
Factor Xa BFP-(factor Xa-sensitive linker)-GFP 385 450 505 1.9 Mitra et al. (1996)
Caspase-3 BFP-(caspase-3-sensitive linker)-GFP 380 440 511 ? Xu et al. (1998)
Ca2+-CaM GFP-CBSM-BFP 380 448 505 5.7 Romoser et al. (1997)
Ca2+ GFP-CBSM-BFP-CaMCN 380 440 505 1.67 Persechini et al. (1997)
Ca2+ ECFP-CaM-M13-EYFP 433 476 527 2.1 Miyawaki et al. (1997, 1999)
Ca2+ ECFP-CaM; M13-EYFP 433 476 527 4 Miyawaki et al. (1997, 1999)
β-Lactamase expression Coumarin-cephalosporin-fluorescein (CCF2) 409 447 520 70 Zlokarnik et al. (1998)
aDonor excitation wavelength, donor emission wavelength, and acceptor emission wavelength, all in nanometers. Small differences (up to 8 nm) in the wavelengths cited by different laboratories for BFP and GFPs are probably not significant.
bMaximum factor by which emission ratio changes from zero to saturating levels of the analyte or process, except for depolarization of 100 mV amplitude.
cHyphens indicate covalent conjugation or fusion. Interacting donor and acceptor molecules are separated by semicolons.
dFRET indicates whether the efficiency of fluorescence resonance energy transfer is increased (↑) or decreased (↓) by the analyte or process.
eTetramethylrhodamine N-hydroxysuccinimide.
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  1. doi:10.1101/pdb.tab1top57 Cold Spring Harb Protoc 2009: pdb.tab1top57-

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