Principles of Fluorescence Spectroscopy

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952 INDEX Time-correlated single-photon counting [cont'd] multichannel analyzer (MCA), 116 photodiodes as, 118–119 pulse pileup, 116–117 time-to-amplitude converter (TAC), 115–116 examples of data, 105–106 laser scanning microscopy, 748–750 light sources, 107–114 femtosecond titanium:sapphire lasers, 108–109 flashlamps, 112–114 laser diodes and light-emitting diodes, 107–108 picosecond dye lasers, 110–112 synchrotron radiation, 114 principles, 104–105 Time-correlated single-photon counting (TCSPC) detectors, 117–121 compact PMTs, 118 Time-dependent anisotropy decays. See Anisotropy decays, time-dependent Time-dependent solvent relaxation, theory of, 250–251 Time-domain decays anisotropy, time-dependent, 383–387 Time-domain lifetime measurements, 97–155 alternative methods for time-resolved measurements, 124–129 microsecond luminescence decays, 129 streak cameras, 125–128 transient recording, 124–125 upconversion methods, 128–129 applications of time-correlated single-photon counting (TCSPC) chlorophyll aggregates in hexane, 146–147 FAD intensity decay, 147–148 green fluorescent protein, systematic data errors, 145–146 picosecond decay time, 146 applications of time-correlated single-photon counting (TSCPC), 145–148 single-tryptophan protein, 145 biopolymers, multi-exponential or heterogeneous decays of, 101–103 data analysis, 129–133 assumptions of nonlinear least-squares method, 130 autocorrelation function, 132–133 goodness of fit (χ R 2), 131–132 least-square analysis, 129–131 maximum entropy method, 148–149 frequency-domain measurements, 98–100 examples of time-domain and frequency-domain lifetimes, 100 lifetime or decay time, meaning of, 99 phase modulation lifetimes, 99–100 global analysis, 144–145 intensity decay laws, 141–144 lifetime distributions, 143 multi-exponential decay, 141–143 stretched exponentials, 144 transient effects, 144–145 multi-exponential decays, analysis of, 133–141 anthranilic acid and 2-aminopurine, 137–138 global analysis, multi-wavelength measurements, 138 goodness of fit comparison, F-statistic, 133–134 number of photon counts, 135, 137 parameter uncertainty-confidence intervals, 134–135, 136 p-terphenyl and indole, 133 resolution of three closely spaced lifetimes, 138–141 vs. steady-state measurements, 97 time-correlated single-photon counting (TCSPC), 103–107 convolution integral, 106–107 examples of data, 105–106 principles, 104–105 time-correlated single-photon counting (TCSPC) detectors, 117–121 color effects in, 119–121 compact PMTs, 118 DNA sequencing, 123–124 dynode chain PMTs, 118 microchannel plate PMTs, 117–118 multi-detector and multidimensional, 121–124 photodiodes as, 118–119 timing effects of monochromators, 121 time-correlated single-photon counting (TCSPC) electronics, 114–117 amplifiers, 115 analyte-to-digital converter (ADC), 115 constant fraction discriminators, 114–115 delay lines, 116 multichannel analyzer (MCA), 116 pulse pileup, 116–117 time-to-amplitude converter (TAC), 115–116 time-correlated single-photon counting (TCSPC) light sources, 107–114 femtosecond titanium:sapphire lasers, 108–109 flashlamps, 112–114 laser diodes and light-emitting diodes, 107–108 picosecond dye lasers, 110–112 synchrotron radiation, 114 Time-domain measurements anisotropy decay, 394–397, 415–417 protein distance distributions from, 487 Time-resolved emission spectra (TRES), 596–597, 598. See also Relaxation dynamics analysis, 246–248 vs. DAS, 255 frequency-domain data for calculation of, 264–265 labeled apomyoglobin, 243–244 membranes, spectral relaxation in, 245–249 overview, 239–240 synthetic fluorescent amino acid, 244–245 Time-resolved emission spectra (TRES) measurement, 240–242 Time-resolved energy transfer. See Energy transfer, time-resolved Time-resolved fluorescence anisotropy decay, 102, 367 Förster distance determination, 499 light sources, 31 principles, 14–15 protein (See Protein fluorescence, time-resolved) reasons for, 14 reversible two-state model, 263–264 Time-resolved fluorescence correlation spectroscopy, 819–820 Time-resolved immunoassays, 659–660 Time-resolved measurements, 779–780 Time-to-amplitude converter (TAC), 104, 105, 115–116, 121, 122 TIN, 715 TIRF, 56 Tissues in-vivo imaging, 656–658 optical properties of, 625 Titanium:sapphire lasers, 108–109, 128, 577 for multiphoton microscopy, 614 TMA, 500–501 TMA-DPH, 72
PRINCIPLES OF FLUORESCENCE SPECTROSCOPY 953 TMR (tetramethylrhodamine), 468 fluorescence intensity distribution analysis, 818, 819 Förster distances, 468 time-resolved fluorescence correlation spectroscopy, 819 TNB (trinitrophenyl) Förster distances, 468 TNS [6-(p-toluidinyl)naphthalene-2-sulfonate] red-edge excitation, 256 vesicles, TRES, 256 TNS [2-(p-toluidinyl)naphthalene-6-sulfonic acid], 71–72 anisotropy decay, 397–398 TNS [6-(p-toluidinyl)naphthalene-2-sulfonic acid], 17–18 TO, 715 TO-8, 118 format of photomultiplier tubes, 46 [2-(p-Toluidinyl)naphthalene-6-sulfonic acid] (TNS). See TNS (2-(p-Toluidinyl)naphthalene-6-sulfonic acid) Total internal reflection (TIR), 56, 760–761, 762, 821–822, 862 literature references, 839 TOTIN, 715 TOTO, 75, 714, 715 Transfer efficiency, 446, 447 Transferrin, energy transfer, 521 Transient effects, time-domain lifetime measurements, 143 Transient recording, 124–125 Transition metal–ligand complexes. See Metal–ligand complexes (MLCs); specific elements Transition moments, anisotropy, 355, 356, 377–378, 433–435 Transit time spreads (TTS), 47, 117–118, 119 Translation diffusion and fluorescence correlation spectroscopy, 802–804 TRES. See Time-resolved emission spectra (TRES) Trichloroethanol (TCE), 278, 292 Trifluoperazine, 89 Trifluoroacetamide (TFA), 288 Trifluoroethanol (TFE), 304 Triosephosphate isomerase, 555, 556 tRNA binding to tRNA synthetase, 370–371 Tropomyosin, 681 Troponin C, 614 calcium-induced conformation changes, 490–493 Troponin I, 589 Trp repressor-DNA binding anisotropy, 373 Trypsin, 368 Tryptophan, 11, 15, 63, 490 absorption and emission spectra, 16, 17 acceptor decay, 489 challenge of, 566–567 conformational changes and accessibility, 288–289 decay-associated emission spectra, 581 emission, 536 emission and protein structure, 560–562 genetically inserted amino-acid analogues, 565–566 tryptophan spectral properties and structural motifs, 561–562 emission in apolar environment, 538–539 emission spectra, 44 energy transfer, 450, 451 excitation polarization spectra, 531–533 frequency-domain lifetime measurements, 188–189 intensity decays, 145, 580–583 multiphoton excitation of, 614 mutants, 552, 555, 556 pH and, 579 phosphorescence of, 598–600 protein fluorescence, 529–530 quantum yield standards, 54 resonance energy transfer in proteins, 540–541, 542 rotamers, 578–579 rotational correlation times, 590 simulated intensity decay, 101–102 solvent effects on emission spectra, 533–534 spectral properties, 530, 531, 561–562 spectral relaxation, 596–598 structure, 579 tryptophan analogs, 562–567 unfolding and exposure to water, 588–589 Tryptophan analogs, protein fluorescence, 562–567 Tryptophan quenching, 279, 280, 283–284, 546–551. See also specific proteins accessibility of quencher, 18, 288, 291, 549–550 emission maxima, effects of, 547–549 emission spectra resolution by, 550–551 endonuclease III, 290–291 localization of membrane-bound residues, 294–295 by phenylalanine, 592–593 quenching constant, 281–282, 548–549 Tryptophan repressor, site-directed mutagenesis, 593–594 Tubulin subunits, 807–808 TU2D, 500–501 Turbidity, 365–366 Twisted internal charge transfer (TICT) state, 207, 220, 221, 627, 645 Two-channel method anisotropy measurement, 363–364 Two-component mixture, global analysis, frequency-domain lifetime measurements, 182–183 Two-photon excitation, 171, 608, 822–823 absorption spectra, 609–610 cross-sections for, 609 diffusion of intracellular kinase, 823 excitation photoselection, 612–613 of fluorophore, 610–612 instrumentation, 21–22 Two-state pH sensors, 637–641 Two-state relaxation, 246, 262–263 model, 237 Tyr-No 2 Förster distances, 468 Tyrosinate-like emissions, 535 Tyrosine, 63, 316 calcium binding to calmodulin using phenylalanine and tyrosine, 545–546 dipeptides, 542 emission from proteins, 535 emission spectra, 44 excitation polarization spectra, 531–533 excited-state ionization of, 534–535 intensity decays, 580–583 protein fluorescence, 529 quantum yield standards, 54 quenchers of, 279 resonance energy transfer in proteins, 540–541, 542, 543–545 spectral properties, 530, 531 structure, 579 vasopressin, 178 Tyrosine kinase, 459 Tyrosine proteins, genetically engineered, 557
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Principles of Fluorescence Spectros
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Joseph R. Lakowicz Center for Fluor
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Preface The first edition of Princi
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x GLOSSARY OF ACRONYMS DNS dansyl o
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xii GLOSSARY OF ACRONYMS TRES time-
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xiv GLOSSARY OF MATHEMATICAL TERMS
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xvi CONTENTS 2.9.4. Conversion betw
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xviii CONTENTS 6. Solvent and Envir
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xx CONTENTS 10.4.4. Alignment of Po
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xxii CONTENTS 14.7.1. Simulations o
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xxiv CONTENTS 19.12. New Approaches
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xxvi CONTENTS 25.3. Optical Propert
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2 INTRODUCTION TO FLUORESCENCE Figu
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6 INTRODUCTION TO FLUORESCENCE inst
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10 INTRODUCTION TO FLUORESCENCE Fig
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12 INTRODUCTION TO FLUORESCENCE ns,
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14 INTRODUCTION TO FLUORESCENCE 1.7
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24 INTRODUCTION TO FLUORESCENCE due
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28 INSTRUMENTATION FOR FLUORESCENCE
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3 Fluorescence probes represent the
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PRINCIPLES OF FLUORESCENCE SPECTROS
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98 TIME-DOMAIN LIFETIME MEASUREMENT
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100 TIME-DOMAIN LIFETIME MEASUREMEN
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5 In the preceding chapter we descr
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6 Solvent polarity and the local en
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238 DYNAMICS OF SOLVENT AND SPECTRA
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278 QUENCHING OF FLUORESCENCE 8.1.
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280 QUENCHING OF FLUORESCENCE Figur
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282 QUENCHING OF FLUORESCENCE ly ev
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290 QUENCHING OF FLUORESCENCE relat
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298 QUENCHING OF FLUORESCENCE σ ar
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320 QUENCHING OF FLUORESCENCE 47. R
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322 QUENCHING OF FLUORESCENCE 113.
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328 QUENCHING OF FLUORESCENCE P8.3.
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330 QUENCHING OF FLUORESCENCE P8.11
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332 MECHANISMS AND DYNAMICS OF FLUO
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10 Measurements of fluorescence ani
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444 ENERGY TRANSFER Figure 13.1. Fl
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446 ENERGY TRANSFER wavelength is e
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448 ENERGY TRANSFER Table 13.1. Cal
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450 ENERGY TRANSFER Figure 13.6. Ab
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452 ENERGY TRANSFER safe for many p
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454 ENERGY TRANSFER Figure 13.12. P
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456 ENERGY TRANSFER Figure 13.16. E
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458 ENERGY TRANSFER Figure 13.21. R
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460 ENERGY TRANSFER Figure 13.24. R
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462 ENERGY TRANSFER tiple acceptors
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464 ENERGY TRANSFER Figure 13.29. A
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466 ENERGY TRANSFER Figure 13.33. F
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468 ENERGY TRANSFER Table 13.3. Rep
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470 ENERGY TRANSFER 55. Clegg RM. 1
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472 ENERGY TRANSFER Tong AK, Jockus
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474 ENERGY TRANSFER Figure 13.39. O
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14 In the previous chapter we descr
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16 The biochemical applications of
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578 TIME-RESOLVED PROTEIN FLUORESCE
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608 MULTIPHOTON EXCITATION AND MICR
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19 Fluorescence sensing of chemical
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676 NOVEL FLUOROPHORES Figure 20.1.
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678 NOVEL FLUOROPHORES Figure 20.7.
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680 NOVEL FLUOROPHORES Figure 20.12
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698 NOVEL FLUOROPHORES 33. Acherman
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700 NOVEL FLUOROPHORES 103. Demas J
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702 NOVEL FLUOROPHORES 176. Montalt
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21 During the past 20 years there h
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22 Fluorescence microscopy is one o
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758 SINGLE-MOLECULE DETECTION Figur
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766 SINGLE-MOLECULE DETECTION small
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770 SINGLE-MOLECULE DETECTION Table
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786 SINGLE-MOLECULE DETECTION face
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788 SINGLE-MOLECULE DETECTION TCSPC
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790 SINGLE-MOLECULE DETECTION 53. H
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792 SINGLE-MOLECULE DETECTION Ke PC
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794 SINGLE-MOLECULE DETECTION Polar
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862 RADIATIVE-DECAY ENGINEERING: SU
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Appendix I Corrected Emission Spect
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Appendix II Fluorescence Lifetime S
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890 APPENDIX III P ADDITIONAL READI
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892 APPENDIX III P ADDITIONAL READI
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894 ANSWERS TO PROBLEMS A1.4. A. Th
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896 ANSWERS TO PROBLEMS Energy tran
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898 ANSWERS TO PROBLEMS Figure 4.65
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