Principles of Fluorescence Spectroscopy

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940 INDEX Membrane-bound fluorophore anisotropy, 353 solvent effects on emission spectra, 215–216 Membrane-bound receptors, 813–815 Membrane fusion and lipid exchange, 465 Membrane potential probes, 72–74 Membrane probes, 72 absorption and emission spectra, 16 anisotropy decay, time-dependent, 401–402 Membranes, 37 acceptor location in lipid vesicles, 521–522 affecting anisotropy, 366 anisotropy, 374–377 distribution of membrane-bound proteins, 375–376 membrane microviscosity, 374–375 anisotropy decay, hindered rotational diffusion in, 399–402 diffusion in lateral, 300–301 diffusive motions in biopolymers, 501 energy transfer, 462–465 lipid distributions around Gramicidin, 463–465 membrane fusion and lipid exchange, 465 relative donor quantum yields, 518 tyrosine-to-tryptophan in membrane-bound protein, 543 multiphoton excitation for membrane-bound fluorophore, 613 phase transitions, 217–219 quenching, 18 boundary lipid, 298 depth-dependent, 296, 297–298 lipid–water partitioning effects, 298–300 localization of tryptophan residues, 294–295 localized quenchers, 295–296 oxygen diffusion, 293–294 parallax quenching in, 296–298 red-edge excitation shifts, 258–259 RET in rapid-diffusion limit retinal location in rhodopsin disk membranes, 522–524 shear stress on viscosity, 225 TNS spectrum, 17–18 TRES, 245–249 Mercaptoacetic acid, 675 Mercury lamps, 33, 38 Merocyanine, 72–73 Metal colloids, optical properties, 845–846 Metal-enhanced fluorescence, 841 applications of, 851–855 DNA hybridization, 853 release of self-quenching, 853–854 silver particles on resonance energy transfer, 854–855 distance dependence of, 851–853 experimental results, 848–851 DNA analysis, 848–851 Jablonski diagram, 842–843 mechanism, 855–856 perspective on, 856 review of, 843–845 theory for fluorophore-colloid interactions, 846–848 Metal ion and anions sensors, 641–643 Metal–ligand complexes (MLCs), 1 energy transfer, 520 frequency-domain lifetime measurements, 174 long-lifetime, 683–695 anisotropy properties, 685–686 biomedical applications, 688–691 energy gap law, 687–688 immunoassays, 691–693 introduction to, 683–685 sensors, 694–695 spectral properties of, 686–687 long-wavelength long-lifetime fluorophores, 695–697 microsecond anisotropy decay, 408–409 oxygen sensors, 627–630 Metalloprotease, 550–551 Metals effects on fluorescence, 843–845 excitation in metal-enhanced fluorescence, 842–843 interactions with fluorophores, 846–848 quenching by, 305 radiative decay engineering, 842 Metal-to-ligand charge transfer (MLCT), 684–685, 687, 694 Metaphase chromosomes, 730 Methanol, 230, 510 dielectric properties, 250 Stokes shift, 209 Methionine, 278, 558 Methionyl-tRNA synthetase, 370–371 Method of moments (MEM), 124, 130 2-Methylanthracene, 293, 294 9-Methylanthracene, 185, 186 N-Methylanthraniloyl amide (NMA), 398 Methyl 8-(2-anthroyl)octanate, 215 Methylindole, 590 Methylmercuric chloride, 279 N-Methylnicotinamide, 278 N-Methylquinolinium iodide (MAI), 306 O-Methyltyrosine, 583 Methylviologen, 309–310, 336, 340, 341 200-MHz fluorometers, 164–165 Micelles, 300 Microbeads, 727, 728 Microchannel plate photomultiplier tubes (PMT), 47, 117–118, 176 Microplate readers, 29–30 Microscopy fluorescence lifetime imaging, 741–752 laser scanning, 748–750 laser scanning confocal, 764 with LED light source, 189 Microsecond anisotropy decays, 408–409 long-lifetime metal-ligand complexes, 408–409 phosphorescence, 408 Microsecond luminescence decays, 129 Microviscosity, membrane, 374–375 Mirror image rule, exceptions to, 8–9 Mixtures fluorescence-lifetime imaging microscopy, 748 quenching-resolved emission spectra, 301–302 sample preparation errors, 57–58 solvent, emission spectra effects, 229–231 TRES and DAS comparison, 255 MLC. See Metal-ligand complexes (MLCs) Mode locking, laser, 110 Modulation lifetimes, 99–100 apparent, 191–192 phase-modulation fluorometry, 198, 266–267 Modulation spectra, 189–191
PRINCIPLES OF FLUORESCENCE SPECTROSCOPY 941 Molecular beacons, 311, 720–724 based on quenching by gold, 723–724 emission spectra, 757–758 with fluorescent acceptors, 722 hybridization proximity beacons, 722–723 intracellular detection of mRNA, 724 with nonfluorescent acceptors, 720–722 quenching by gold colloids, 313–314 quenching by gold surface, 314, 315 single-molecule detection, 782 Molecular biology quenching applications, 310–313 Molecular chaperonin cpn60 (GroEL), 371 Molecular information from fluorescence, 17–19 emission spectra and Stokes shift, 17–18 fluorescence polarization of anisotropy, 19 quenching, 18–19 resonance energy transfer, 19 Molecular weight effect on diffusion coefficients, 806–807 Moments and higher orders literature references, 838 Monellin, 548 anisotropy decay, 432, 588 phosphorescence, 599 Monochromators, 28, 34–35 instrumentation calibration of, 38 polarization characteristics of, 36 second-order transmission in, 37 stray light in, 36–37 time-correlated single-photon counting, 121 wavelength resolution and emission spectra, 35 Monte Carlo simulations energy transfer, 517 parameter uncertainty, 135 Motions of molecular motors, 784 MQAE [N-(ethyoxycarbonylmethyl)-6-methoxyquinolinium], 79, 632 MR121, 311, 782 mRNA intracellular detection of by molecular beacons, 724 M13 peptide, single-molecule calcium sensor, 784 Multi-alkali photocathode, 46 Multichannel analyzer (MCA), 116, 121 Multicolor fluorescence in-situ hybridization (m-FISH), 731 Multi-exponential decay emission center of gravity, 583 frequency-domain lifetime measurements, 171, 178–186 global analysis of two-component mixture, 182–183 maximum entropy analysis, 185–186 melittin, 171 three-component mixture, resolution limits, 183–185 three-component mixture, resolution of 10-fold range of decay times, 185 two closely spaced lifetimes, 180–182 two widely spaced lifetimes, 178–180 multi-tryptophan proteins, 584 resolution, 103 solvent effects, 229–231 time-domain lifetime measurements, 133–141 anthranilic acid and 2-aminopurine, 137–138 global analysis, multi-wavelength measurements, 138 goodness of fit comparison, F-statistic, 133–134 intensity decay laws, 141–143 multi-exponential or heterogeneous decays of, 101–103 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 Multi-exponential phosphorescence, 599 Multi-exponential relaxation measurement, 252–253 in water, 251–252 Multiphoton excitation, 607–619, 822 cross-sections for, 609 instrumentation, 21–22 of intrinsic protein fluorescence, 613–616 for membrane-bound fluorophore, 613 microscopy, 616–619 calcium imaging, 616–617 excitation of multiple fluorophores, 618 imaging of NAD(P)H and FAD, 617–618 three-dimensional imaging of cells, 618–619 two-photon absorption spectra, 609–610 two-photon excitation of fluorophore, 610–612 Multiphoton excitation anisotropy, 612–613 Multiphoton microscopy, 607, 616–619 calcium imaging, 616–617 excitation of multiple fluorophores, 618 imaging of NAD(P)H and FAD, 617–618 three-dimensional imaging of cells, 618–619 Multiple decay time quenching, 291 Multiple intensity decay, 122 Multiplexed microbead arrays:suspension arrays, 726–727, 728 Multiplex-FISH, 731 Multiscalars, 129 Multi-wavelength excitation, time-dependent anisotropy decay, 429–430 Myb oncoprotein, 553–554 Myelin basic protein, 548 Myoglobin, 243, 584, 596 Myosin light-chain kinase (MLCK), 372, 456–457 Myosin S-1, 452 Myosin S-1 subfragment, 770–771 N NADH, 16, 63–65 frequency-domain lifetime measurements, 172, 177, 178 imaging of, multiphoton microscopy, 617–618 protein binding, 65–67 quenching by adenine moiety, 278 Nanoengineering, surface plasmon-coupled emission, 870 Nanoparticles lanthanides, 682 protein binding to, 457–458 semiconductor, 675–678 Nanosecond flashlamp, 112–113 Naphthalene, 279 Förster distances, 468 1,8-Naphthalimide, 340, 341 Naphthalocyanines, 75 Naphthol dissociation, time-domain studies of, 264–265 excited-state reactions, 260–262 Naphthyl-2-acetyl, 495 Naphthylamine derivatives, 213
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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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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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578 TIME-RESOLVED PROTEIN FLUORESCE
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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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Page 895 and 896: PRINCIPLES OF FLUORESCENCE SPECTROS
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