Fluorescence Quenching: Theory and Applications

Solute fluorescence quenching reactions were first applied to biochemical problems in the late 1960s and early 1970s, 7) and since that time they have been a very valuable research tool for studies with proteins, membranes, and other macromolecular assemblies. Quenching reactions are easy to perform, require only a small sample, usually are nondestructive, and can be applied to almost any system that has an intrinsic or extrinsic fluorescence probe. The most important characteristic, however, is the value of the information that these reactions can provide. Solute quenching reactions, using quenchers such as molecular oxygen, acrylamide, or iodide ion, provide information about the location of fluorescent groups in a macromolecular structure. A fluorophore that is located on the surface of a larger structure will be relatively accessible to a solute quencher that is dissolved in the aqueous phase. A fluorophore that is removed from the surface of a structure will be quenched to a lesser degree by the quencher. Thus, the quenching reaction can be used to probe topographical features of a macromolecular assembly and to sense any structural changes that may be caused by varying conditions or the addition of reagents. In addition, quenching reactions can, in some situations, provide information about conformational fluctuations. In Sections 2.3 and 2.4 I will discuss several examples of the use of solute quenchers in studies with proteins, membranes, and nucleic acids. Solute fluorescence quenching reactions can also be used to selectively alter the fluorescence properties of a sample in order to resolve contributions or aid in the measurement of data. To elaborate on this point, consider the different characteristics of fluorescence: the quantum yield, excitation and

[1]  M. Steinberg,et al.  Accessibility of tryptophan residues in Na,K-ATPase. , 1987, The Journal of biological chemistry.

[2]  W. Wintermeyer,et al.  Incorporation of 1,N6-ethenoadenosine into the 3' terminus of tRNA using T4 RNA ligase. 2. Preparation and ribosome interaction of fluorescent Escherichia coli tRNAMetf. , 1984, European journal of biochemistry.

[3]  F. Teale,et al.  Depolarization of the intrinsic and extrinsic fluorescence of pepsinogen and pepsin. , 1970, The Biochemical journal.

[4]  M. Ruwart,et al.  Activation of yeast pyruvate kinase by natural and artificial cryoprotectants. , 1971, The Journal of biological chemistry.

[5]  S. Lehrer.  Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. , 1971, Biochemistry.

[6]  M. Raftery,et al.  Direct spectroscopic studies of cation translocation by Torpedo acetylcholine receptor on a time scale of physiological relevance. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[7]  J. Parks,et al.  Fluorescence quenching by the stable free radical di‐t‐butylnitroxide , 1973 .

[8]  K. Ghiggino,et al.  The transverse location of tryptophan residues in the purple membranes of Halobacterium halobium studied by fluorescence quenching and energy transfer , 1984 .

[9]  G. Sanyal,et al.  Probable role of amphiphilicity in the binding of mastoparan to calmodulin. , 1985, Biochemistry.

[10]  W. Hillen,et al.  Engineered Tet repressor mutants with single tryptophan residues as fluorescent probes. Solvent accessibilities of DNA and inducer binding sites and interaction with tetracycline. , 1987, The Journal of biological chemistry.

[11]  B F Anderson,et al.  Structure of azurin from Alcaligenes denitrificans at 2.5 A resolution. , 1983, Journal of molecular biology.

[12]  W. Stryjewski,et al.  The resolution of heterogeneous fluorescence of multitryptophan-containing proteins studied by a fluorescence-quenching method. , 1986, European journal of biochemistry.

[13]  J. Keizer.  Effect of diffusion on reaction rates in solution and in membranes , 1981 .

[14]  M. Eftink,et al.  Does the fluorescence quencher acrylamide bind to proteins? , 1987, Biochimica et biophysica acta.

[15]  C A Ghiron,et al.  Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. , 1976, Biochemistry.

[16]  R. Kretsinger,et al.  Carp muscle calcium-binding protein. II. Structure determination and general description. , 1973, The Journal of biological chemistry.

[17]  R. F. Chen.  Quenching of the fluorescence of proteins by silver nitrate. , 1973, Archives of biochemistry and biophysics.

[18]  J. Lakowicz,et al.  Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. , 1973, Biochemistry.

[19]  B. Maliwal,et al.  Rotational freedom of tryptophan residues in proteins and peptides. , 1983, Biochemistry.

[20]  B. de Kruijff,et al.  Penetration of a cardiotoxin into cardiolipin model membranes and its implications on lipid organization. , 1985, Biochemistry.

[21]  Long Jw,et al.  Transfer of singlet energy within trypsin. , 1979 .

[22]  E. Gratton,et al.  A model of dynamic quenching of fluorescence in globular proteins. , 1984, Biophysical journal.

[23]  E. London,et al.  Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. , 1987, Biochemistry.

[24]  J. Callis,et al.  Pyrene. A probe of lateral diffusion in the hydrophobic region of membranes. , 1974, Biochemistry.

[25]  E. Lissi,et al.  Evaluation of partition constants in compartmentalised systems from fluorescence quenching data , 1982 .

[26]  H. Pownall,et al.  Fluorescence quenching of anthracene in charged micelles by pyridinium and iodide ions. , 1974, Biochemistry.

[27]  D. James,et al.  Distributions of fluorescence lifetimes: consequences for the photophysics of molecules adsorbed on surfaces , 1985 .

[28]  L. McLean,et al.  Effect of micelle diameter on tryptophan dynamics in an amphipathic helical peptide in phosphatidylcholine. , 1989, Biochemistry.

[29]  M. D. De Wolf,et al.  pH-induced transitions in cholera toxin conformation: a fluorescence study. , 1987, Biochemistry.

[30]  B. Somogyi,et al.  Gated quenching of intrinsic fluorescence and phosphorescence of globular proteins. An extended model. , 1986, Biophysical journal.

[31]  H. Asai,et al.  Structural difference between two ATP-binding sites of heavy meromyosin revealed by the dynamic fluorescence quenching technique. , 1984, Biochimica et biophysica acta.

[32]  K. Muczynski,et al.  Incorporation of danyslated phospholipids and dehydroergosterol into membranes using a phospholipid exchange protein. , 1983, Biochemistry.

[33]  J. Loscalzo,et al.  Conformational domains and structural transitions of human von Willebrand protein. , 1984, Biochemistry.

[34]  R. Chatelier,et al.  Effects of quenching mechanism and type of quencher association on stern-volmer plots in compartmentalized systems. , 1986, Biophysical journal.

[35]  J. Barber,et al.  A method for estimating lateral diffusion coefficients in membranes from steady-state fluorescence quenching studies. , 1987, Biophysical journal.

[36]  C. Ghiron,et al.  Acrylamide quenching studies with azurin B , 1981 .

[37]  J. Yguerabide,et al.  KINETICS OF DIFFUSION-CONTROLLED PROCESSES IN LIQUIDS. THEORETICAL CONSIDERATION OF LUMINESCENT SYSTEMS: QUENCHING AND EXCITATION TRANSFER IN COLLISION , 1964 .

[38]  J. K. Thomas,et al.  Dynamics of Pyrene Fluorescence in Phospholipid Dispersions , 1974 .

[39]  A. Gafni.  Accessibility of adenine binding sites in dehydrogenases to small molecules studied by fluorescence quenching. , 1979, Biochemistry.

[40]  B. Maliwal,et al.  Nanosecond motions of the single tryptophan residues in apolipoproteins C-I and C-II: a study by oxygen quenching and fluorescence depolarization. , 1985, Archives of Biochemistry and Biophysics.

[41]  Michael L. Johnson,et al.  [16] Nonlinear least-squares analysis , 1985 .

[42]  M. Battino,et al.  Determination of partition and lateral diffusion coefficients of ubiquinones by fluorescence quenching of n-(9-anthroyloxy)stearic acids in phospholipid vesicles and mitochondrial membranes. , 1986, Biochemistry.

[43]  M. Eftink,et al.  Viscosity dependence of the solute quenching of the tryptophanyl fluorescence of proteins. , 1986, Biophysical chemistry.

[44]  G. Porter,et al.  Oxygen quenching of aromatic triplet states in solution. Part 1 , 1973 .

[45]  M. Karplus,et al.  Dynamics of ligand binding to heme proteins. , 1979, Journal of molecular biology.

[46]  S. Georghiou,et al.  Melittin-phospholipid interaction: evidence for melittin aggregation. , 1981, Biochimica et biophysica acta.

[47]  G. Feigenson,et al.  Fluorescence quenching in model membranes. 1. Characterization of quenching caused by a spin-labeled phospholipid. , 1981, Biochemistry.

[48]  M. Beltramini,et al.  Emission quenching mechanisms in Octopus vulgaris hemocyanin: steady-state and time-resolved fluorescence studies , 1987 .

[49]  Raymond F. Chen,et al.  Biochemical fluorescence : concepts , 1975 .

[50]  M. Eftink,et al.  Fluorescence quenching of indole and model micelle systems , 1976 .

[51]  J. Lakowicz,et al.  Diffusion and partitioning of a pesticide, lindane, into phosphatidylcholine bilayers. A new fluorescence quenching method to study chlorinated hydrocarbon-membrane interactions. , 1977, Biochimica et Biophysica Acta.

[52]  G. Fleming,et al.  Picosecond time-resolved fluorescence of ribonuclease T1. A pH and substrate analogue binding study. , 1987, Biophysical journal.

[53]  F. Richards.  Packing defects, cavities, volume fluctuations, and access to the interior of proteins. Including some general comments on surface area and protein structure , 1979 .

[54]  J. Lakowicz,et al.  PICOSECOND RESOLUTION OF INDOLE ANISOTROPY DECAYS AND SPECTRAL RELAXATION BY 2 GHz FREQUENCY‐DOMAIN FLUOROMETRY , 1988, Photochemistry and photobiology.

[55]  D. Wallach,et al.  Variations of lipid-protein interactions in erythrocyte ghosts as a function of temperature and pH in physiological and non-physiological ranges. A study using a paramagnetic quenching of protein fluorescence by nitroxide lipid analogues. , 1975, Biochimica et biophysica acta.

[56]  H. Möhwald,et al.  Monitoring the location profile of fluorophores in phosphatidylcholine bilayers by the use or paramagnetic quenching. , 1979, Biochimica et biophysica acta.

[57]  M. Shinitzky,et al.  Degree of exposure of membrane proteins determined by fluorescence quenching. , 1977, Biochemistry.

[58]  S. Englander,et al.  Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence. , 1983, Biochemistry.

[59]  I Munro,et al.  Subnanosecond motions of tryptophan residues in proteins. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[60]  R. Cukier.  On the quencher concentration dependence of fluorescence quenching: The role of solution dielectric constant and ionic strength , 1985 .

[61]  A. Edwards,et al.  Exposure of tryptophanyl residues in alpha-lactalbumin and lysozyme. Quantitative determination by fluorescence quenching studies. , 1986, Radiation and environmental biophysics.

[62]  P. Torgerson.  Tryptophan emission from myosin subfragment 1: acrylamide and nucleotide effect monitored by decay-associated spectra. , 1984, Biochemistry.

[63]  P. Froehlich,et al.  Fluorescence quenching of indoles by amides , 1978 .

[64]  D. Kearns,et al.  Role of Singlet Excited States of Molecular Oxygen in the Quenching of Organic Triplet States , 1967 .

[65]  K. Thulborn,et al.  Comparison of fluorescence energy transfer and quenching methods to establish the position and orientation of components within the transverse plane of the lipid bilayer. Application to the gramicidin A--bilayer interaction. , 1979, Biochemistry.

[66]  George E. Kimball,et al.  Diffusion-controlled reaction rates , 1949 .

[67]  M. Eftink,et al.  Fluorescence quenching studies with proteins. , 1981, Analytical biochemistry.

[68]  G. Strambini.  Singular oxygen effects on the room-temperature phosphorescence of alcohol dehydrogenase from horse liver. , 1983, Biophysical journal.

[69]  M. Eftink,et al.  Frequency domain measurements of the fluorescence lifetime of ribonuclease T1. , 1987, Biophysical journal.

[70]  H Frauenfelder,et al.  Solvent viscosity and protein dynamics. , 1980, Biochemistry.

[71]  M. Monsigny,et al.  Fluorescence quenching of tryptophan by trifluoroacetamide. , 1984, Biochimica et biophysica acta.

[72]  E. Gratton,et al.  Oxygen distribution and migration within Mbdes Fe and Hbdes Fe. Multifrequency phase and modulation fluorometry study. , 1984, Biophysical Journal.

[73]  Z. Wasylewski,et al.  Frequency-domain fluorescence studies of an extracellular metalloproteinase of Staphylococcus aureus. , 1987, Biochimica et biophysica acta.

[74]  D. Thomas,et al.  Electrical excitability of artificial enzyme membranes. III. Hysteresis and oscillations observed with immobilized acetylcholinesterase membranes. , 1982, Biophysical chemistry.

[75]  D. A. Labianca,et al.  Structure-reactivity factors in the quenching of fluorescence from naphthalenes by conjugated dienes , 1972 .

[76]  C. Pande,et al.  Characterization of the fluorescent bimane derivative of E. coli initiator transfer RNA (tRNAfMet). , 1985, Biochemical and biophysical research communications.

[77]  A. Tappel,et al.  Determination by fluorescence quenching of the environment of DNA crosslinks made by malondialdehyde. , 1983, Biochimica et biophysica acta.

[78]  G. Omann,et al.  Dynamic quenchers in fluorescently labeled membranes. Theory for quenching in a three-phase system. , 1985, Biophysical journal.

[79]  W. Mantulin,et al.  Fluorescence quenching studies of apolipoprotein A-I in solution and in lipid-protein complexes: protein dynamics. , 1986, Biochemistry.

[80]  A. Spisni,et al.  Intermolecular interactions of gramicidin A' transmembrane channels incorporated into lysophosphatidylcholine lipid systems. , 1982, Biochimica et biophysica acta.

[81]  J. Lakowicz,et al.  Enhanced resolution of fluorescence anisotropy decays by simultaneous analysis of progressively quenched samples. Applications to anisotropic rotations and to protein dynamics. , 1987, Biophysical journal.

[82]  E. Gratton,et al.  Intrinsic fluorescence of elongation factor Tu in its complexes with GDP and elongation factor Ts. , 1987, Biochemistry.

[83]  H. Scheraga,et al.  Thermodynamics of the quenching of tyrosyl fluorescence by dithiothreitol. , 1987, Biochemistry.

[84]  D. Wallach,et al.  Lipid-protein relationships in erythrocyte membranes revealed by paramagnetic quenching of protein fluorescence. , 1976, Biochimica et biophysica acta.

[85]  C. Cantor,et al.  Studies on the conformation of the anticodon loop of phenylalanine transfer ribonucleic acid. Effect of environment on the fluorescence of the Y base. , 1970, Biochemistry.

[86]  J. Lakowicz,et al.  Acrylamide quenching of Yt-base fluorescence in aqueous solution. , 1988, Biophysical chemistry.

[87]  P. Luisi,et al.  Fluorescence quenching and energy transfer in complexes between horse-liver alcohol dehydrogenase and coenzymes. , 1978, European journal of biochemistry.

[88]  P. Horowitz,et al.  Detection, characterization, and quenching of the intrinsic fluorescence of bovine heart cytochrome c oxidase. , 1986, Biochemistry.

[89]  S. McLaughlin,et al.  An experimental test of the discreteness-of-charge effect in positive and negative lipid bilayers. , 1986, Biochemistry.

[90]  R. Verrall,et al.  THREE EXPONENTIAL FLUORESCENCE DECAY OF HORSE LIVER ALCOHOL DEHYDROGENASE REVEALED BY IODIDE QUENCHING , 1987, Photochemistry and photobiology.

[91]  C. Woodward,et al.  Hydrogen exchange and the dynamic structure of proteins , 1982, Molecular and Cellular Biochemistry.

[92]  M. Eftink,et al.  Fluorescence quenching of the buried tryptophan residue of cod parvalbumin. , 1985, Biophysical chemistry.

[93]  F. Mérola,et al.  Quenching by acrylamide and temperature of a fluorescent probe attached to the active site of Ribonuclease , 2004, European Biophysics Journal.

[94]  P. Humphries,et al.  Observations on the structure of two human 7SK pseudogenes and on homologous transcripts in vertebrate species. , 1987, The Biochemical journal.

[95]  Raymond F. Chen.  Fluorescene Difference Decay Curves: Resolution Of Complex Decays , 1984 .

[96]  M. Eftink,et al.  Indole fluorescence quenching studies on proteins and model systems: use of the inefficient quencher succinimide , 1984 .

[97]  B. Maliwal,et al.  Oxygen quenching and fluorescence depolarization of tyrosine residues in proteins. , 1983, The Journal of biological chemistry.

[98]  C. Hélène,et al.  TYROSINE ENVIRONMENT AND PHOSPHATE BINDING IN THE ARCHAEBACTERIAL HISTONE-LIKE PROTEIN HTA , 1988 .

[99]  Joseph R. Lakowicz,et al.  Time-resolved laser spectroscopy in biochemistry II , 1990 .

[100]  K. Thulborn,et al.  Properties and the locations of a set of fluorescent probes sensitive to the fluidity gradient of the lipid bilayer. , 1978, Biochimica et biophysica acta.

[101]  J. Lakowicz,et al.  Transient Effects in Fluorescence Quenching Measured by 2-GHz Frequency-Domain Fluorometry. , 1987, The Journal of physical chemistry.

[102]  A. Szabó,et al.  Diffusion-controlled bimolecular reaction rates. The effect of rotational diffusion and orientation constraints. , 1981, Biophysical journal.

[103]  G. Kneale,et al.  Time resolved fluorescence of bacteriophage Pfl DNA binding protein and its complex with DNA , 2004, European Biophysics Journal.

[104]  A. Chaffotte,et al.  Fluorescence-quenching studies on a conformational transition within a domain of the beta 2 subunit of Escherichia coli tryptophan synthase. , 1984, European journal of biochemistry.

[105]  G. Strambini.  Quenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structure. , 1987, Biophysical journal.

[106]  T. Tao,et al.  Fluorescence lifetime quenching studies on the accessibilities of actin sulfhydryl sites. , 1979, Biochemistry.

[107]  P. Bartlett,et al.  A general model for dispersed kinetics in heterogeneous systems , 1985 .

[108]  F. Castelli,et al.  Lifetime and quenching of tryptophan fluorescence in whiting parvalbumin. , 1988, Biochemistry.

[109]  H. Asai,et al.  Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. , 1981, Journal of biochemistry.

[110]  S. Lehrer.  The selective quenching of tryptophan fluorescence in proteins by iodide ion: lysozyme in the presence and absence of substrate. , 1967, Biochemical and biophysical research communications.

[111]  Jay R. Knutson,et al.  Simultaneous analysis of multiple fluorescence decay curves: A global approach , 1983 .

[112]  S. Narasimhulu.  Quenching of tryptophanyl fluorescence of bovine adrenal P-450C-21 and inhibition of substrate binding by acrylamide. , 1988, Biochemistry.

[113]  Lawson Wr,et al.  The mechanism of quenching of liver alcohol dehydrogenase fluorescence due to ternary complex formation. , 1978 .

[114]  A. Kleinfeld.  Tryptophan imaging of membrane proteins. , 1985, Biochemistry.

[115]  B. Maliwal,et al.  Effect of ligand binding and conformational changes in proteins on oxygen quenching and fluorescence depolarization of tryptophan residues. , 1984, Biophysical Chemistry.

[116]  E. Blatt,et al.  The association of acrylamide with proteins. The interpretation of fluorescence quenching experiments. , 1986, Biochimica et biophysica acta.

[117]  J. Baird,et al.  Fluorescence Quenching at High Quencher Concentrations , 1983 .

[118]  D. Cowan,et al.  Photochemical reactions. V. Photodimerization of acenaphthylene. Heavy-atom solvent effects , 1970 .

[119]  J. Lakowicz.  Principles of fluorescence spectroscopy , 1983 .

[120]  B. Valeur,et al.  RESOLUTION OF THE FLUORESCENCE EXCITATION SPECTRUM OF INDOLE INTO THE 1La AND 1Lb EXCITATION BANDS * , 1977, Photochemistry and photobiology.

[121]  A. Zlotnick,et al.  Fluorescence quenching of cytochrome b5 in vesicles with an asymmetric transbilayer distribution of brominated phosphatidylcholine. , 1986, The Journal of biological chemistry.

[122]  M. Eftink,et al.  Fluorescence quenching of liver alcohol dehydrogenase by acrylamide. , 1982, Biochemistry.

[123]  Z. Wasylewski,et al.  Phase-resolved spectral measurements with several two tryptophan containing proteins. , 1987, Biochemistry.

[124]  R. Steiner,et al.  The interaction of the ground and excited states of indole derivatives with electron scavengers. , 1969, The Journal of physical chemistry.

[125]  D. Desilets,et al.  Improved method for determination of Stern-Volmer quenching constants , 1987 .

[126]  M. Eftink,et al.  Fluorescence quenching of Trp-314 of liver alcohol dehydrogenase by oxygen. , 1984, Biophysical chemistry.

[127]  F. C. Hartman,et al.  Fluorescence studies of phosphoribulokinase, a light-regulated, chloroplastic enzyme. , 1988, Archives of biochemistry and biophysics.

[128]  M. Barkley,et al.  Tryptophan fluorescence of terminal deoxynucleotidyl transferase: effects of quenchers on time-resolved emission spectra. , 1985, Biochemistry.

[129]  S. Lehrer,et al.  [10] Solute quenching of protein fluorescence , 1978 .

[130]  D. Johnson,et al.  Solute accessibility to N epsilon-fluorescein isothiocyanate-lysine-23 cobra alpha-toxin bound to the acetylcholine receptor. A consideration of the effect of rotational diffusion and orientation constraints on fluorescence quenching. , 1985, Biophysical journal.

[131]  K. Gekko,et al.  Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. , 1981, Biochemistry.

[132]  L. Stryer,et al.  Diffusion-enhanced fluorescence energy transfer. , 1982, Annual review of biophysics and bioengineering.

[133]  Eftink Mr,et al.  Acrylamide and oxygen fluorescence quenching studies with liver alcohol dehydrogenase using steady-state and phase fluorometry , 1982 .

[134]  R. Santus,et al.  DETERMINATION OF THE ACRYLAMIDE QUENCHING CONSTANT FOR PROTEIN AND MODEL INDOLE TRIPLETS , 1988, Photochemistry and Photobiology.

[135]  C. Ghiron,et al.  ROLE OF THE TRYPTOPHAN FLUORESCENT STATE IN THE ULTRAVIOLET‐INDUCED INACTIVATION OF β‐TRYPSIN* , 1973 .

[136]  D. E. Olins,et al.  Nonhistone chromosomal protein HMG 1 interactions with DNA. Fluorescence and thermal denaturation studies. , 1985, The Journal of biological chemistry.

[137]  J. Zajicek,et al.  A hydrophobic quencher of protein fluorescence: 2,2,2-trichloroethanol. , 1977, Biochimica et biophysica acta.

[138]  M. Eftink,et al.  Fluorescence lifetime and anisotropy studies with liver alcohol dehydrogenase and its complexes. , 1986, Biochemistry.

[139]  A. Watkins.  Kinetics of fluorescence quenching by inorganic anions , 1974 .

[140]  Douglas R. James,et al.  A fallacy in the interpretation of fluorescence decay parameters , 1985 .

[141]  D. Gérard,et al.  ACRYLAMIDE FLUORESCENCE QUENCHING APPLIED TO TYROSYL RESIDUES IN PROTEINS , 1983, Photochemistry and photobiology.

[142]  T. Schleich,et al.  Assessment of the exposure and environments of tryptophanyl residues in ribosomal protein S1 by fluorescence quenching. , 1981, Biochemistry.

[143]  J. Keizer.  Theory of rapid bimolecular reactions in solution and membranes , 1985 .

[144]  M. Eftink,et al.  Exposure of tryptophanyl residues and protein dynamics. , 1977, Biochemistry.

[145]  C. Gerday,et al.  Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy. , 1985, Archives of biochemistry and biophysics.

[146]  E Gratton,et al.  Fluorescence lifetime distributions in proteins. , 1987, Biophysical journal.

[147]  S. N. Timasheff,et al.  Preferential binding of solvent components to proteins in mixed water--organic solvent systems. , 1968, Biochemistry.

[148]  R. Epand,et al.  Fluorescence studies on a membrane-embedded peptide from the carboxy terminus of lipophilin. , 1986, Biochemistry.

[149]  Z. Wasylewski,et al.  STUDIES OF THE EFFICIENCY and MECHANISM OF FLUORESCENCE QUENCHING REACTIONS USING ACRYLAMIDE and SUCCINIMIDE AS QUENCHERS , 1987 .

[150]  M. Friedman.  Solvent effects in reactions of amino groups in amino acids, peptides, and proteins with alpha, beta-unsaturated compounds. , 1967, Journal of the American Chemical Society.

[151]  J. Gomez-Fernandez,et al.  A fluorescence quenching study of tryptophanyl residues of (Ca2+ + Mg2+)-ATPase from sarcoplasmic reticulum. , 1985, The Journal of biological chemistry.

[152]  B. Somogyi,et al.  A double-quenching method for studying protein dynamics: separation of the fluorescence quenching parameters characteristic of solvent-exposed and solvent-masked fluorophors. , 1985, Biochemistry.

[153]  E. A. Burstein,et al.  FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULES , 1973, Photochemistry and photobiology.

[154]  E. Hayon,et al.  Excited state chemistry of aromatic amino acids and related peptides. III. Tryptophan. , 1975, Journal of the American Chemical Society.

[155]  D. O'Kane,et al.  Determination of rotational correlation times from deconvoluted fluorescence anisotropy decay curves. Demonstration with 6,7-dimethyl-8-ribityllumazine and lumazine protein from Photobacterium leiognathi as fluorescent indicators. , 1985, Biochemistry.

[156]  G. Sanyal,et al.  Tryptophan fluorescence studies of subunit interaction and rotational dynamics of human luteinizing hormone. , 1987, Biochemistry.

[157]  G. Feigenson,et al.  Protein redistribution in model membranes: clearing of M13 coat protein from calcium-induced gel-phase regions in phosphatidylserine/phosphatidylcholine multilamellar vesicles. , 1987, Biochemistry.

[158]  A. Kleinfeld,et al.  Interaction of fluorescence quenchers with the n-(9-anthroyloxy) fatty acid membrane probes , 1983 .

[159]  J J Volwerk,et al.  Complex photophysics of the single tryptophan of porcine pancreatic phospholipase A2, its zymogen, and an enzyme/micelle complex. , 1985, Biochemistry.

[160]  N. Kallenbach,et al.  Hydrogen exchange and structural dynamics of proteins and nucleic acids , 1983, Quarterly Reviews of Biophysics.

[161]  T. M. Devlin,et al.  Effects of lipid fluidity on quenching characteristics of tryptophan fluorescence in yeast plasma membrane. , 1982, The Journal of biological chemistry.

[162]  U. Heinemann,et al.  Specific protein-nucleic acid recognition in ribonuclease T1–2′-guanylic acid complex: an X-ray study , 1982, Nature.

[163]  T. Tao,et al.  Fluorescence lifetime and acrylamide quenching studies of the interactions between troponin subunits. , 1984, Biochemistry.

[164]  M L Saviotti,et al.  Room temperature phosphorescence and the dynamic aspects of protein structure. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[165]  J. Brochon,et al.  Dynamics of peptide - nucleic acid complexes. Fluorescence polarization studies. , 1982, Biochimie.

[166]  J. Lakowicz,et al.  Effect of pressure on the self-association of melittin. , 1984, Biochemistry.

[167]  J. Andre,et al.  Kinetics of partly diffusion controlled reactions. I. Transient and apparent transient effect in fluorescence quenching , 1978 .

[168]  N. Geacintov,et al.  ACRYLAMIDE AND MOLECULAR OXYGEN FLUORESCENCE QUENCHING AS A PROBE OF SOLVENT‐ACCESSIBILITY OF AROMATIC FLUOROPHORES COMPLEXED WITH DNA IN RELATION TO THEIR CONFORMATIONS: CORONENE‐DNA AND OTHER COMPLEXES , 1988, Photochemistry and photobiology.

[169]  G. Fleming,et al.  Internal motion and electron transfer in proteins: a picosecond fluorescence study of three homologous azurins. , 1987, Biochemistry.

[170]  C. Owen.  Two dimensional diffusion theory: Cylindrical diffusion model applied to fluorescence quenching , 1975 .

[171]  Joseph R. Lakowicz,et al.  2-GHz frequency-domain fluorometer , 1986 .

[172]  A. R. Horrocks,et al.  Mechanism of fluorescence quenching in solution. Part 2.—Quenching by xenon and intersystem crossing efficiencies , 1966 .

[173]  G. Durocher,et al.  HOW HYDROGEN BONDING OF CARBAZOLE TO ETHANOL AFFECTS ITS FLUORESCENCE QUENCHING RATE BY ELECTRON ACCEPTOR QUENCHER MOLECULES , 1981 .

[174]  W. DeGrado,et al.  Fluorescence properties of calmodulin-binding peptides reflect alpha-helical periodicity. , 1987, Science.

[175]  J. B. Birks,et al.  Organic Molecular Photophysics , 1975 .

[176]  A. Jonas,et al.  Nanosecond rotational motions of apolipoprotein C-I in solution and in complexes with dimyristoylphosphatidylcholine. , 1982, Biochemistry.

[177]  A. Muhlrad,et al.  Modification of myosin subfragment 1 tryptophans by dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide. , 1987, Biochemistry.

[178]  S. Englander,et al.  Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence. , 1983, Biochemistry.

[179]  W. Ware,et al.  Kinetics of diffusion‐controlled reactions: Transient effects in fluorescence quenching , 1975 .

[180]  R. F. Evans,et al.  FLASH PHOTOLYSIS OF TRYPTOPHAN AND N‐ACETYL‐L‐TRYPTOPHANAMIDE; THE EFFECT OF BROMIDE ON TRANSIENT YIELDS , 1977 .

[181]  J. A. Wells,et al.  Characterization of the properties of ethenoadenosine nucleotides bound or trapped at the active site of myosin subfragment 1. , 1984, Biochemistry.

[182]  J. Beechem,et al.  Global resolution of heterogeneous decay by phase/modulation fluorometry: mixtures and proteins , 1983 .

[183]  C. J. Schmidt,et al.  Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. , 1981, Biochemistry.

[184]  J. Toulmé,et al.  Role of tryptophyl residues in the binding of gene 32 protein from phage T4 to single-stranded DNA. Photochemical modification of tryptophan by trichloroethanol , 1984 .

[185]  S. Cockle,et al.  TIME‐RESOLVED FLUORESCENCE SPECTRA OF TRYPTOPHAN IN MONOMERIC GLUCAGON * , 1981, Photochemistry and photobiology.

[186]  G. Weber,et al.  Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan and related compounds. , 1960, The Biochemical journal.

[187]  G. Johnson.  Fluorescence quenching of carbazoles , 1980 .

[188]  S. Englander,et al.  On the prevalence of room-temperature protein phosphorescence. , 1987, Science.

[189]  T. E. Thompson,et al.  Oxygen quenching of pyrene-lipid fluorescence in phosphatidylcholine vesicles. A probe for membrane organization. , 1985, Biophysical journal.

[190]  E Gratton,et al.  Interpretation of fluorescence decays in proteins using continuous lifetime distributions. , 1987, Biophysical journal.

[191]  J. Feitelson,et al.  Quenching of the zinc-protoporphyrin triplet state as a measure of small-molecule diffusion through the structure of myoglobin. , 1987, Biochemistry.

[192]  J. Lakowicz,et al.  End-to-end distance distributions of flexible molecules from steady state fluorescence energy transfer and quenching-induced changes in the Förster distance , 1988 .

[193]  R. Verrall,et al.  Fluorescence lifetime quenching and anisotropy studies of ribonuclease T1. , 1985, Biochemistry.

[194]  E. Permyakov,et al.  Investigation of some physico-chemical properties of muscular parvalbumins by means of the luminescence of their phenylalanyl residues. , 1975, Biochimica et biophysica acta.

[195]  A. Lane.  The accessibility of the active site and conformation states of the beta 2 subunit of tryptophan synthase studied by fluorescence quenching. , 1983, European journal of biochemistry.

[196]  M. Eftink.  Quenching-resolved emission anisotropy studies with single and multitryptophan-containing proteins. , 1983, Biophysical journal.

[197]  E. Blatt,et al.  Depth-dependent fluorescent quenching in micelles and membranes. , 1985, Biochimica et biophysica acta.

[198]  K. Imakubo,et al.  TEMPERATURE DEPENDENCE OF THE PHOSPHORESCENCE LIFETIMES OF HETEROGENEOUS TRYPTOPHAN RESIDUES IN GLOBULAR PROTEINS BETWEEN 293 AND 77 K , 1979 .

[199]  J M Beechem,et al.  Time-resolved fluorescence of proteins. , 1985, Annual review of biochemistry.

[200]  A. Philips,et al.  Immunoaffinity purification and fluorescence studies of human adenosine deaminase. , 1987, Biochemistry.

[201]  G. Weber,et al.  Oxygen quenching of pyrenebutyric acid fluorescence in water. A dynamic probe of the microenvironment. , 1970, Biochemistry.

[202]  R. Santus,et al.  Determination of the dioxygen quenching constant for protein and model indole triplets. , 1988, Biochimica et biophysica acta.

[203]  J. Lakowicz,et al.  Hindered depolarizing rotations of perylene in lipid bilayers. Detection by lifetime-resolved fluorescence anisotropy measurements. , 1980, Biochemistry.

[204]  M. D. De Wolf,et al.  Tryptophan residues of cholera toxin and its A and B protomers. Intrinsic fluorescence and solute quenching upon interacting with the ganglioside GM1, oligo-GM1, or dansylated oligo-GM1. , 1981, The Journal of biological chemistry.

[205]  R. V. Resandt.  Picosecond transient effect in the fluorescence quenching of tryptophan , 1983 .

[206]  Aleksandr Petrovich Demchenko,et al.  Ultraviolet Spectroscopy of Proteins , 1986, 1987.

[207]  A. Stone,et al.  Excited‐State Intermolecular Interactions Involving Paramagnetic Molecules: Effect of Spin—Spin and Spin—Orbit Interactions on the Quenching of Triplets , 1971 .

[208]  S. Verjovski-Almeida,et al.  Labeling of a thiol residue in sarcoplasmic reticulum ATPase by pyrene maleimide. Solvent accessibility studied by fluorescence quenching. , 1985, The Journal of biological chemistry.

[209]  M. Eftink,et al.  Dynamics of a protein matrix revealed by fluorescence quenching. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[210]  G Weber,et al.  The effect of high pressure upon proteins and other biomolecules , 1983, Quarterly Reviews of Biophysics.

[211]  John R. Miller,et al.  Effect of free energy on rates of electron transfer between molecules. [Pulsed irradiation] , 1984 .

[212]  J. Kägi,et al.  Tryptophan residues of creatine kinase: a fluorescence study. , 1985, Biochemistry.

[213]  A. Zlotnick,et al.  Determination of the topography of cytochrome b5 in lipid vesicles by fluorescence quenching. , 1985, Biochemistry.

[214]  R. A. Badley.  The location of protein in serum lipoproteins: a fluorescence quenching study. , 1975, Biochimica et biophysica acta.

[215]  Ludwig Brand,et al.  Global analysis of fluorescence decay surfaces: excited-state reactions , 1985 .

[216]  S. Atherton,et al.  Quenching of the fluorescence of DNA-intercalated ethidium bromide by some transition-metal ions , 1986 .

[217]  J. Lakowicz,et al.  Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. , 1973, Biochemistry.

[218]  D. Yang,et al.  Methionyl-tRNA synthetase induced 3'-terminal and delocalized conformational transition in tRNAfMet: steady-state fluorescence of tRNA with a single fluorophore. , 1986, Biochemistry.

[219]  H. Dekkers,et al.  Fluorescence studies on the coat protein of alfalfa mosaic virus. , 1986, Journal of biomolecular structure & dynamics.