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Journal articles on the topic 'Intrinsic protein fluorescence'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 April 2022

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1

Goldberg, Jacob M., Rebecca F. Wissner, Alyssa M. Klein, and E. James Petersson. "Thioamide quenching of intrinsic protein fluorescence." Chemical Communications 48, no. 10 (2012): 1550–52. http://dx.doi.org/10.1039/c1cc14708k.

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2

Brewis, Neil, Anne Phelan, Jeanette Webb, Jeff Drew, Gill Elliott, and Peter O'Hare. "Evaluation of VP22 Spread in Tissue Culture." Journal of Virology 74, no. 2 (January 15, 2000): 1051–56. http://dx.doi.org/10.1128/jvi.74.2.1051-1056.2000.

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ABSTRACT We compare methods of detection of intercellular transport of the herpes simplex virus protein VP22 and of a green fluorescent protein (GFP)-VP22 fusion protein. Spread of both proteins was observed by immunofluorescence (IF) using organic fixatives. Spread of both proteins was also detected by IF after paraformaldehyde (PFA) fixation and detergent permeabilization, albeit at reduced levels. However, while spread of GFP-VP22 was observed by examining intrinsic GFP fluorescence after methanol fixation, little spread was observed after PFA fixation, suggesting that the levels of the fusion protein in recipient cells were below the detection limits of intrinsic-fluorescence or that PFA fixation quenches the fluorescence of GFP-VP22. We further considered whether elution of VP22 from methanol-fixed cells and postfixation binding to surrounding cells contributed to the increased detection of spread observed after methanol fixation. The results show that while this could occur, it appeared to be a minor effect not accounting for the observed VP22 cell-to-cell spread in culture.

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3

Goldberg, Jacob M., Rebecca F. Wissner, Alyssa M. Klein, and E. James Petersson. "Correction: Thioamide quenching of intrinsic protein fluorescence." Chemical Communications 56, no. 25 (2020): 3699. http://dx.doi.org/10.1039/d0cc90120b.

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4

Meyer, Arne, Christian Betzel, and Marc Pusey. "Latest methods of fluorescence-based protein crystal identification." Acta Crystallographica Section F Structural Biology Communications 71, no. 2 (January 28, 2015): 121–31. http://dx.doi.org/10.1107/s2053230x15000114.

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Successful protein crystallization screening experiments are dependent upon the experimenter being able to identify positive outcomes. The introduction of fluorescence techniques has brought a powerful and versatile tool to the aid of the crystal grower. Trace fluorescent labeling, in which a fluorescent probe is covalently bound to a subpopulation (<0.5%) of the protein, enables the use of visible fluorescence. Alternatively, one can avoid covalent modification and use UV fluorescence, exploiting the intrinsic fluorescent amino acids present in most proteins. By the use of these techniques, crystals that had previously been obscured in the crystallization drop can readily be identified and distinguished from amorphous precipitate or salt crystals. Additionally, lead conditions that may not have been obvious as such under white-light illumination can be identified. In all cases review of the screening plate is considerably accelerated, as the eye can quickly note objects of increased intensity.

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5

Schlick, Kristian H., Candace K. Lange, Gregory D. Gillispie, and Mary J. Cloninger. "Characterization of Protein Aggregation via Intrinsic Fluorescence Lifetime." Journal of the American Chemical Society 131, no. 46 (November 25, 2009): 16608–9. http://dx.doi.org/10.1021/ja904073p.

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6

Duysak, Taner, Thanh Tuyen Tran, Aqeel Rana Afzal, and Che-Hun Jung. "Fluorescence Spectroscopic Analysis of ppGpp Binding to cAMP Receptor Protein and Histone-Like Nucleoid Structuring Protein." International Journal of Molecular Sciences 22, no. 15 (July 23, 2021): 7871. http://dx.doi.org/10.3390/ijms22157871.

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The cyclic AMP receptor protein (CRP) is one of the best-known transcription factors, regulating about 400 genes. The histone-like nucleoid structuring protein (H-NS) is one of the nucleoid-forming proteins and is responsible for DNA packaging and gene repression in prokaryotes. In this study, the binding of ppGpp to CRP and H-NS was determined by fluorescence spectroscopy. CRP from Escherichia coli exhibited intrinsic fluorescence at 341 nm when excited at 280 nm. The fluorescence intensity decreased in the presence of ppGpp. The dissociation constant of 35 ± 3 µM suggests that ppGpp binds to CRP with a similar affinity to cAMP. H-NS also shows intrinsic fluorescence at 329 nm. The fluorescence intensity was decreased by various ligands and the calculated dissociation constant for ppGpp was 80 ± 11 µM, which suggests that the binding site was occupied fully by ppGpp under starvation conditions. This study suggests the modulatory effects of ppGpp in gene expression regulated by CRP and H-NS. The method described here may be applicable to many other proteins.

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7

Ferreira, Sérgio T., and Tatiana Coelho-Sampaio. "Intrinsic fluorescence as a probe of structure-function relationships in Ca2+-transport ATPases." Bioscience Reports 16, no. 2 (April 1, 1996): 87–106. http://dx.doi.org/10.1007/bf01206199.

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Applications of intrinsic fluorescence measurements in the study of Ca2+-transport ATPases are reviewed. Since the initial reports showing that the fluorescence emission was sensitive to Ca2+ binding, a substantial amount of work has focused on the use of both steady-state and time-resolved fluorescence spectroscopy to investigate structure-function relationships in sarcoplasmic reticulum and plasma membrane Ca2+-ATPases. These studies have revealed ligand-induced conformational changes, as well as provided information on protein-protein, protein-solvent and/or protein-lipid interactions in different functional states of these proteins. The main results of these studies, as well as possible future prospects are discussed.

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8

Thaa, Bastian, Andreas Herrmann, and Michael Veit. "Intrinsic Cytoskeleton-Dependent Clustering of Influenza Virus M2 Protein with Hemagglutinin Assessed by FLIM-FRET." Journal of Virology 84, no. 23 (September 29, 2010): 12445–49. http://dx.doi.org/10.1128/jvi.01322-10.

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ABSTRACT The hemagglutinin (HA) of influenza virus organizes the virus bud zone, a domain of the plasma membrane enriched in raft lipids. Using fluorescence lifetime imaging microscopy-fluorescence resonance energy transfer (FLIM-FRET), a technique that detects close colocalization of fluorescent proteins in transfected cells, we show that the viral proton channel M2 clusters with HA but not with a marker for inner leaflet rafts. The FRET signal between M2 and HA depends on the raft-targeting signals in HA and on an intact actin cytoskeleton. We conclude that M2 contains an intrinsic signal that targets the protein to the viral bud zone, which is organized by raft-associated HA and by cortical actin.

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9

Stapelfeldt, Henrik, and Leif H. Skibsted. "Modification of β–lactoglobulin by aliphatic aldehydes in aqueous solution." Journal of Dairy Research 61, no. 2 (May 1994): 209–19. http://dx.doi.org/10.1017/s0022029900028223.

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SummaryEach of the secondary lipid oxidation products pentanal, hexanal and heptanal was found to react with β–lactoglobulin (β–lg) in a two-phase model System (aqueous phosphate buffer–1-octanol) yielding fluorescent condensation products (emission maximum, 410 nm; excitation maximum, 350 nm). Protein polymers were detected by size-exclusion HPLC, and the rate of reaction paralleled the formation of fluorescent products, with the reactivity being pentanal > hexanal > heptanal. Simultaneously, the reaction also changed the intrinsic fluorescence of β–lg, and in particular pentanal reduced the intensity of tryptophan fluorescence (emission maximum, 332 nm; excitation maximum, 288 nm) by 30%. These findings are discussed with reference to the effect of peroxidizing lipids on the physical properties of whey proteins and the use of protein fluorescence (induced by the reaction with aldehydes) as marker for the oxidative status of milk and whey protein products.

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10

Okerberg, Eric, and Jason B. Shear. "Attomole-Level Protein Fingerprinting Based on Intrinsic Peptide Fluorescence." Analytical Chemistry 73, no. 7 (April 2001): 1610–13. http://dx.doi.org/10.1021/ac0012703.

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11

Chan, Fiona T. S., Gabriele S. Kaminski Schierle, Janet R. Kumita, Carlos W. Bertoncini, Christopher M. Dobson, and Clemens F. Kaminski. "Protein amyloids develop an intrinsic fluorescence signature during aggregation." Analyst 138, no. 7 (2013): 2156. http://dx.doi.org/10.1039/c3an36798c.

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12

Rosato, Nicola, Giampiero Mei, Isabella Savini, Franco Del Bolgia, Alessandro Finazzi-Agrò, Arjen Lommen, and Gerard W. Canters. "Intrinsic fluorescence of the bacterial copper-containing protein amicyanin." Archives of Biochemistry and Biophysics 284, no. 1 (January 1991): 112–15. http://dx.doi.org/10.1016/0003-9861(91)90271-j.

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13

BUCHE, André, Carmen MÉNDEZ, and José A. SALAS. "Interaction between ATP, oleandomycin and the OleB ATP-binding cassette transporter of Streptomyces antibioticus involved in oleandomycin secretion." Biochemical Journal 321, no. 1 (January 1, 1997): 139–44. http://dx.doi.org/10.1042/bj3210139.

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The OleB protein of Streptomyces antibioticus, oleandomycin (OM) producer, constitutes an ATP-binding cassette transporter containing two nucleotide-binding domains and is involved in OM resistance and its secretion in this producer strain. We have characterized some properties of the first nucleotide-binding domain of OleB using an overexpressed fusion protein (MBP–OleB´) between a maltose-binding protein (MBP) and the first half of OleB (OleB´). Extrinsic fluorescence of the base-modified fluorescent nucleotide analogue 1,N6-ethenoadenosine 5´-triphosphate (εATP) and 2´(3´)-o-(2,4,6-trinitrophenyl)adenosine-5´-triphosphate was determined in the presence of MBP and the fusion protein MBP–OleB´, and it was found that εATP binds to MBP–OleB´ with a stoichiometry of 0.9. Measurements of the intrinsic fluorescence of the MBP–OleB´ fusion protein indicated that ATP induces a decrease in the accessibility of the MBP–OleB´ tryptophans to acrylamide, an indication of a folding effect. This conclusion was confirmed by the fact that ATP also induces considerable stabilization against guanidine chloride denaturation of MBP–OleB´. Two effects were found to be associated with the presence of Mg2+ ions: (1) an increase in the quenching of MBP–OleB´ intrinsic fluorescence by ATP; and (2) an increase in the accessibility of MBP–OleB´ tryptophans to acrylamide. Significant changes in the intrinsic fluorescence of the fusion protein were also observed in the presence of OM, demostrating the existence of interaction between the transporter and the antibiotic in the absence of any hydrophobic membrane component.

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14

STARIKOV, EVGENI B., ITAI PANAS, YUJI MOCHIZUKI, SHIGENORI TANAKA, YI LUO, and HANS ÅGREN. "ON MECHANISM OF ENHANCED FLUORESCENCE IN GREEN FLUORESCENT PROTEIN." Biophysical Reviews and Letters 02, no. 03n04 (October 2007): 221–27. http://dx.doi.org/10.1142/s1793048007000568.

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In spite of the numerous experimental and theoretical studies on green fluorescent protein and its modifications, there is still no definitive answer to the central question: why such systems exhibit enhanced fluorescence. Based upon detailed quantum-chemical estimations, we advocate the following hypothesis. In the green fluorescent protein ground electronic state, the protein surrounding strains the chromophore with respect to its native intramolecular conformational preference in vacuo or in solution. Absorbing a photon of the proper wavelength not only causes a joint proton–electron transfer in and around the chromophore, but also increases the intrinsic strain of the latter. Since conformational relaxation of such a structure will not require any additional energy input, the energy gained by the chromophore cannot be dissipated into the chromophore's internal non-radiative degrees of freedom, and thus it returns as a fluorescence emission.

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15

Svendsen, Annette, Hjalte V. Kiefer, Henrik B. Pedersen, Anastasia V. Bochenkova, and Lars H. Andersen. "Origin of the Intrinsic Fluorescence of the Green Fluorescent Protein." Journal of the American Chemical Society 139, no. 25 (June 19, 2017): 8766–71. http://dx.doi.org/10.1021/jacs.7b04987.

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16

Molla, Anisur R., and Pritha Mandal. "Study of Organization and Dynamics of Multi-Tryptophan Protein Molecules Utilizing Red Edge Excitation Shift Approach." Asian Journal of Chemistry 32, no. 10 (2020): 2416–22. http://dx.doi.org/10.14233/ajchem.2020.22785.

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A shift in the fluorescence emission maxima with gradual increase in excitation wavelength is termed as red edge excitation shift (REES). Tryptophan residues are widely utilized as intrinsic fluorescence probe to investigate the protein structures. Wavelength selective tryptophan fluorescence can explore the dynamics of surrounded water molecules, the ubiquitous biological solvent. Thus REES experiment of various protein conformational states can provide significant input to the study of protein folding pathway and it can also be useful to study interaction of proteins with others. In this review article, we shall focus on red edge effect of various multi-tryptophan proteins in their respective native, intermediate and denatured state.

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17

Casals, C., E. Miguel, and J. Perez-Gil. "Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles." Biochemical Journal 296, no. 3 (December 15, 1993): 585–93. http://dx.doi.org/10.1042/bj2960585.

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The fluorescence characteristics of surfactant protein A (SP-A) from porcine and human bronchoalveolar lavage were determined in the presence and absence of lipids. After excitation at either 275 or 295 nm, the fluorescence emission spectrum of both proteins was characterized by two maxima at about 326 and 337 nm, indicating heterogeneity in the emission of the two tryptophan residues of SP-A, and also revealing a partially buried character for these fluorophores. Interaction of both human and porcine SP-A with various phospholipid vesicles resulted in an increase in the fluorescence emission of tryptophan without any shift in the emission wavelength maxima. This change in intrinsic fluorescence was found to be more pronounced in the presence of dipalmitoyl phosphatidylcholine (DPPC) than with dipalmitoyl phosphatidylglycerol (DPPG), DPPC/DPPG (7:3, w/w) and 1-palmitoyl-sn-glycerol-3-phosphocholine (LPC). Intrinsic fluorescence of SP-A was almost completely unaffected in the presence of egg phosphatidylcholine (egg-PC). In addition, we demonstrated a shielding of the tryptophan fluorescence from quenching by acrylamide on interaction of porcine SP-A with DPPC, DPPG or LPC. This shielding was most pronounced in the presence of DPPC. In the case of human SP-A, shielding was only observed on interaction with DPPC. From the intrinsic fluorescence measurements as well as from the quenching experiments, we concluded that the interaction of some phospholipid vesicles with SP-A produces a conformational change on the protein molecule and that the interaction of SP-A with DPPC is stronger than with other phospholipids. This interaction appeared to be independent of Ca2+ ions. Physiological ionic strength was found to be required for the interaction of SP-A with negatively charged vesicles of either DPPG or DPPC/DPPG (7:3, w/w). Intrinsic fluorescence of SP-A was sensitive to the physical state of the DPPC vesicles. The increase in intrinsic fluorescence of SP-A in the presence of DPPC vesicles was much stronger when the vesicles were in the gel state than when they were in the liquid-crystalline state. The effect produced by SP-A on the lipid vesicles was also dependent on temperature. The aggregation of DPPC, DPPC/DPPG (7:3, w/w) or dimyristoyl phosphatidylglycerol (DMPG) was many times higher below the phase-transition temperature of the corresponding phospholipids. These results strongly indicate that the interaction of SP-A with phospholipid vesicles requires the lipids to be in the gel phase.

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18

Hubmann, M. R., M. J. Leiner, and R. J. Schaur. "Ultraviolet fluorescence of human sera: I. Sources of characteristic differences in the ultraviolet fluorescence spectra of sera from normal and cancer-bearing humans." Clinical Chemistry 36, no. 11 (November 1, 1990): 1880–83. http://dx.doi.org/10.1093/clinchem/36.11.1880.

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Abstract The ultraviolet fluorescence emission spectra of sera from apparently healthy persons and of sera from cancer patients frequently show significantly different curve shapes. A biparametric fluorescence method has been developed to use these deviations to detect patients with malignant diseases (Clin Chem 1986;32:1974-8). However, the pathobiochemical reasons for these differences of diagnostic importance have thus far been unclear. To find a relevant explanation for the described effect, we focused our interest on human serum proteins, the materials mainly responsible for the intrinsic fluorescence of sera in this spectral region. Human sera of various protein compositions were selected according to their protein pattern, determined by cellulose acetate electrophoresis, and their intrinsic fluorescence properties were investigated. We found that the emission spectra of human sera were correlated with their relative protein compositions, albumin and alpha-2 globulins being the most significantly correlated with the fluorescence intensity ratios. Because increased percentages of alpha-2 globulins and decreased percentages of albumin frequently accompany malignancies, we suggest that this condition accounts for the differences between the emission spectra of sera from normal and cancer-bearing humans.

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19

Lukk, Tiit, Richard E. Gillilan, Doletha M. E. Szebenyi, and Warren R. Zipfel. "A visible-light-excited fluorescence method for imaging protein crystals without added dyes." Journal of Applied Crystallography 49, no. 1 (February 1, 2016): 234–40. http://dx.doi.org/10.1107/s160057671502419x.

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Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting protein crystals in screening trays. The fluorescence-based crystal detection methods have thus far relied on intrinsic UV-inducible tryptophan fluorescence, nonlinear optics or fluorescence in the visible light range dependent on crystals soaked with fluorescent dyes. In this paper data are presented on a novel visible-light-inducible autofluorescence arising from protein crystals as a result of general stabilization of conjugated double-bond systems and increased charge delocalization due to crystal packing. The visible-light-inducible autofluorescence serves as a complementary method to bright-field microscopy in beamline applications where accurate crystal centering about the rotation axis is essential. Owing to temperature-dependent chromophore stabilization, protein crystals exhibit tenfold higher fluorescence intensity at cryogenic temperatures, making the method ideal for experiments where crystals are cooled to 100 K with a cryostream. In addition to the non-damaging excitation wavelength and low laser power required for imaging, the method can also serve a useful role for differentiating protein crystals from salt crystals in screening trays.

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20

Li, Chenghui, Peng Wu, and Xiandeng Hou. "Plasma-assisted quadruple-channel optosensing of proteins and cells with Mn-doped ZnS quantum dots." Nanoscale 8, no. 7 (2016): 4291–98. http://dx.doi.org/10.1039/c5nr09130f.

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The addition of the intrinsic fluorescence of proteins to the existing triple-channel optical properties of Mn–ZnS QDs yields new quadruple-channel optosensing devices with substantially increased discrimination capacity for proteins. A low-temperature plasma for protein treatment further enforces the discrimination.

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21

Tuparev, Nikolai, Anelia Dobrikova, Stefka Taneva, and Tzvetana Lazarova. "Bacteriorhodopsin Thermal Stability: Influence of Bound Cations and Lipids on the Intrinsic Protein Fluorescence." Zeitschrift für Naturforschung C 55, no. 5-6 (June 1, 2000): 355–60. http://dx.doi.org/10.1515/znc-2000-5-610.

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Temperature - induced changes in protein intrinsic fluorescence of native, delipidated and deionized purple membranes are investigated. It is found that the removal of cations most strongly affects the protein and its thermal stability. The denaturation of dei-BR completes at 70 °C, while delipidated and native BR still maintain their native structure at this temperature. Both, the quantum yield and the fluorescence maximum suggest correlation between the Trp-retinal coupling and protein structural stability. The low red shift of the fluorescence maximum caused by increasing of temperature indicates limited unfolding of bacteriorhodopsin upon denaturation.

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22

Maji, Samir K., Jason J. Amsden, Kenneth J. Rothschild, Margaret M. Condron, and David B. Teplow. "Conformational Dynamics of Amyloid β-Protein Assembly Probed Using Intrinsic Fluorescence†." Biochemistry 44, no. 40 (October 2005): 13365–76. http://dx.doi.org/10.1021/bi0508284.

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23

Bayram, Serene S., Philippe Green, and Amy Szuchmacher Blum. "Sensing of heavy metal ions by intrinsic TMV coat protein fluorescence." Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 195 (April 2018): 21–24. http://dx.doi.org/10.1016/j.saa.2018.01.035.

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24

Asanov, Alexander N., Heather M. McDonald, Philip B. Oldham, Mark J. Jedrzejas, and W. William Wilson. "Intrinsic fluorescence as a potential rapid scoring tool for protein crystals." Journal of Crystal Growth 232, no. 1-4 (November 2001): 603–9. http://dx.doi.org/10.1016/s0022-0248(01)01093-4.

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25

Ikematsu, Mineo, Daizo Takaoka, and Masashi Yasuda. "Odorant Binding to Bovine Odorant Binding Protein Detected by Intrinsic Fluorescence." Chemistry Letters 34, no. 9 (September 2005): 1256–57. http://dx.doi.org/10.1246/cl.2005.1256.

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26

Matthieu, Gaudet, Remtulla Nina, Jackson Sophie E., Main Ewan R. G., Bracewell Daniel G., Aeppli Gabriel, and Dalby Paul A. "Protein denaturation and protein:drugs interactions from intrinsic protein fluorescence measurements at the nanolitre scale." Protein Science 19, no. 8 (June 15, 2010): 1544–54. http://dx.doi.org/10.1002/pro.433.

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27

Goldberg, Jacob M., and E. James Petersson. "Thioamide Quenching of Intrinsic and Extrinsic Protein Fluorescence: Minimalist Tools for Studying Protein Dynamics." Biophysical Journal 102, no. 3 (January 2012): 403a. http://dx.doi.org/10.1016/j.bpj.2011.11.2202.

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28

Raines, Douglas E., and Katie B. McClure. "Halothane Interactions with Nicotinic Acetylcholine Receptor Membranes." Anesthesiology 86, no. 2 (February 1, 1997): 476–86. http://dx.doi.org/10.1097/00000542-199702000-00023.

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Background Although it has been suggested that anesthetics alter protein conformational states by binding to nonpolar sites within the interior regions of proteins, the rate and extent to which anesthetics penetrate membrane proteins has not been characterized. The authors report the use of steady-state and stopped-flow spectroscopy to characterize the interactions of halothane with receptor membranes. Methods Steady-state and stopped-flow fluorescence spectroscopy was used to characterize halothane quenching of nicotinic acetylcholine receptor (nAcChoR)-rich membrane intrinsic fluorescence and the rate of isoflurane-induced nAcChoR desensitization. Results At equilibrium, halothane quenched only 54 +/- 1.4% of all tryptophan fluorescence. Diethyl ether failed to reduce fluorescence quenching by halothane, suggesting that it does not bind to the same protein sites as halothane. Stopped-flow fluorescence traces defined two kinetic components of quenching: a fast component that occurred in less than 1 ms followed by a slower biphasic fluorescence decay. Protein unfolding with sodium dodecyl sulfate reduced halothane's Stern-Volmer quenching constant, eliminated the biphasic decay, and rendered fluorescence accessible to quenching by halothane within 1 ms. Functional studies indicate that anesthetic-induced desensitization of nAcChoR occurs in less than 2 ms. Conclusions Unquenchable fluorescence arises from tryptophan residues that are buried within the protein and protected from halothane. Sodium dodecyl sulfate unfolds membrane proteins and allows previously buried fluorescence protein residues to be rapidly and homogeneously quenched by halothane. Halothane quenches protein components of nAcChoR membranes over the same concentration range and time scale that it exerts its functional effects, a finding that is generally consistent with a protein site of action.

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29

Voicescu, Mariana, and Sorana Ionescu. "3-hydroxyflavone-bovine serum albumin interaction in Dextran medium." Journal of the Serbian Chemical Society 80, no. 4 (2015): 517–28. http://dx.doi.org/10.2298/jsc140425075v.

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Spectroscopic analysis of a bioactive flavonol, 3-Hydroxyflavone (3-HF), in systems based on Dextran 70 (Dx70) (an important bio-relevant polysacharide) and Bovine Serum Albumin (BSA) (a carrier protein), have been studied by fluorescence and circular dichroism. Changes produced by different concentrations of Dx70 on the fluorescent characteristics of 3-HF, and on the excited - state intramolecular proton transfer (ESIPT) process were studied. The influence of 3-HF binding and of Dx70 on the secondary structure of BSA were investigated by circular dichroism spectroscopy. The influence of temperature (30-80?C range) on the intrinsic Tryptophan fluorescence in 3-HF/BSA/Dx70 systems, was investigated. The results are discussed with relevance to 3-HF as a sensitive fluorescence probe for exploring flavone-protein interaction in plasma expander media and also for its biological evaluation.

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30

Roper, Jason M., Rhonda J. Staversky, Jacob N. Finkelstein, Peter C. Keng, and Michael A. O'Reilly. "Identification and isolation of mouse type II cells on the basis of intrinsic expression of enhanced green fluorescent protein." American Journal of Physiology-Lung Cellular and Molecular Physiology 285, no. 3 (September 2003): L691—L700. http://dx.doi.org/10.1152/ajplung.00034.2003.

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The unique morphology and cell-specific expression of surfactant genes have been used to identify and isolate alveolar type II epithelial cells. Because these attributes can change during lung injury, a novel method was developed for detecting and isolating mouse type II cells on the basis of transgenic expression of enhanced green fluorescence protein (EGFP). A line of transgenic mice was created in which EGFP was targeted to type II cells under control of the human surfactant protein (SP)-C promoter. Green fluorescent cells that colocalized by immunostaining with endogenous pro-SP-C were scattered throughout the parenchyma. EGFP was not detected in Clara cell secretory protein-expressing airway epithelial cells or other nonlung tissues. Pro-SP-C immunostaining diminished in lungs exposed to hyperoxia, consistent with decreased expression and secretion of intracellular precursor protein. In contrast, type II cells could still be identified by their intrinsic green fluorescence, because EGFP is not secreted. Type II cells could also be purified from single-cell suspensions of lung homogenates using fluorescence-activated cell sorting. Less than 1% of presorted cells exhibited green fluorescence compared with >95% of the sorted population. As expected for type II cells, ultrastructural analysis revealed that the sorted cells contained numerous lamellar bodies. SP-A, SP-B, and SP-C mRNAs were detected in the sorted population, but T1α and CD31 (platelet endothelial cell adhesion molecule) were not, indicating enrichment of type II epithelial cells. This method will be invaluable for detecting and isolating mouse type II cells under a variety of experimental conditions.

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Baek, M., W. H. Nelson, P. E. Hargraves, J. F. Tanguay, and S. L. Suib. "The Steady-State and Decay Characteristics of Protein Tryptophan Fluorescence from Algae." Applied Spectroscopy 42, no. 8 (November 1988): 1405–12. http://dx.doi.org/10.1366/0003702884429599.

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The intrinsic steady-state fluorescence due to tryptophan has been obtained from monospecific cultures of fourteen plankton algae of various genera. Fluorescence decay profiles of protein tryptophan residues were obtained for eight marine plankton algae. Each organism exhibits a strong maximum in its emission spectrum at 320–340 nm when excited at 290 nm. Iodide quenching and denaturization experiments with 8 M urea provide strong evidence for the assignment of the 320–340 nm fluorescence to protein tryptophan. Most importantly, the decay of this bacterial protein tryptophan fluorescence has been described. The observation that characteristic protein-tryptophan fluorescence lifetimes have been obtained for each organism suggests that measurements of fluorescence lifetimes may be helpful in the rapid characterization of algae. Direct application will likely be found in combination with the measurement of other luminescence parameters.

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32

Tiwari, Prince. "Fluorescence-based Techniques to Study the Structure and Dynamics of Mass-selected Biomolecular Ions." CHIMIA International Journal for Chemistry 75, no. 4 (April 28, 2021): 252–56. http://dx.doi.org/10.2533/chimia.2021.252.

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Laser-induced fluorescence studies on mass-selected biomolecules are a promising route to understand their properties in the gas phase and probe their intrinsic properties in a solvent-free environment. Fluorescence has been used to investigate the conformation and dynamics of gaseous biomolecular ions. With Förster Resonance Energy Transfer (FRET), it is now possible to obtain sensitive intramolecular distance information from large biomolecules, like proteins, with high chemical specificity. With growing interest and applications, gas-phase fluorescence measurements can shed greater light on the characteristics of proteins in the gas phase. Compared to the solution phase measurements, gas-phase fluorescence can also help understand the influence of solvent interactions on the protein structure and function.

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33

Challa, Pavan Kumar, Quentin Peter, Maya A. Wright, Yuewen Zhang, Kadi L. Saar, Jacqueline A. Carozza, Justin L. P. Benesch, and Tuomas P. J. Knowles. "Real-Time Intrinsic Fluorescence Visualization and Sizing of Proteins and Protein Complexes in Microfluidic Devices." Analytical Chemistry 90, no. 6 (February 16, 2018): 3849–55. http://dx.doi.org/10.1021/acs.analchem.7b04523.

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34

Apter, B., N. Lapshina, H. Barhom, B. Fainberg, A. Handelman, A. Accardo, C. Diaferia, P. Ginzburg, G. Morelli, and G. Rosenman. "Fluorescence Phenomena in Amyloid and Amyloidogenic Bionanostructures." Crystals 10, no. 8 (August 3, 2020): 668. http://dx.doi.org/10.3390/cryst10080668.

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Nanoscale optical labeling is an advanced bioimaging tool. It is mostly based on fluorescence (FL) phenomena and enables the visualization of single biocells, bacteria, viruses, and biological tissues, providing monitoring of functional biosystems in vitro and in vivo, and the imaging-guided transportation of drug molecules. There is a variety of FL biolabels such as organic molecular dyes, genetically encoded fluorescent proteins (green fluorescent protein and homologs), semiconductor quantum dots, carbon dots, plasmonic metal gold-based nanostructures and more. In this review, a new generation of FL biolabels based on the recently found biophotonic effects of visible FL are described. This intrinsic FL phenomenon is observed in any peptide/protein materials folded into β-sheet secondary structures, irrespective of their composition, complexity, and origin. The FL effect has been observed both in natural amyloid fibrils, associated with neurodegenerative diseases (Alzheimer’s, Parkinson’s, and more), and diverse synthetic peptide/protein structures subjected to thermally induced biological refolding helix-like→β-sheet. This approach allowed us to develop a new generation of FL peptide/protein bionanodots radiating multicolor, tunable, visible FL, covering the entire visible spectrum in the range of 400–700 nm. Newly developed biocompatible nanoscale biomarkers are considered as a promising tool for emerging precise biomedicine and advanced medical nanotechnologies (high-resolution bioimaging, light diagnostics, therapy, optogenetics, and health monitoring).

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35

Zhai, Xiuhong, Margarita L. Malakhova, Helen M. Pike, Linda M. Benson, H. Robert Bergen, István P. Sugár, Lucy Malinina, Dinshaw J. Patel, and Rhoderick E. Brown. "Glycolipid Acquisition by Human Glycolipid Transfer Protein Dramatically Alters Intrinsic Tryptophan Fluorescence." Journal of Biological Chemistry 284, no. 20 (March 7, 2009): 13620–28. http://dx.doi.org/10.1074/jbc.m809089200.

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36

Pokalsky, Christine, Peter Wick, Etti Harms, Fred E. Lytle, and Robert L. Van Etten. "Fluorescence Resolution of the Intrinsic Tryptophan Residues of Bovine Protein Tyrosyl Phosphatase." Journal of Biological Chemistry 270, no. 8 (February 24, 1995): 3809–15. http://dx.doi.org/10.1074/jbc.270.8.3809.

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37

Anderle, Heinz, and Alfred Weber. "Fluorescent rare earth solutions as intrinsic wavelength standards for protein fluorescence spectroscopy." Analytical Biochemistry 518 (February 2017): 86–88. http://dx.doi.org/10.1016/j.ab.2016.11.011.

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38

Sharkey, Lisa M., Nathaniel Safren, Amit S. Pithadia, Julia E. Gerson, Mark Dulchavsky, Svetlana Fischer, Ronak Patel, et al. "Mutant UBQLN2 promotes toxicity by modulating intrinsic self-assembly." Proceedings of the National Academy of Sciences 115, no. 44 (October 17, 2018): E10495—E10504. http://dx.doi.org/10.1073/pnas.1810522115.

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UBQLN2 is one of a family of proteins implicated in ubiquitin-dependent protein quality control and integrally tied to human neurodegenerative disease. Whereas wild-type UBQLN2 accumulates in intraneuronal deposits in several common age-related neurodegenerative diseases, mutations in the gene encoding this protein result in X-linked amyotrophic lateral sclerosis/frontotemporal dementia associated with TDP43 accumulation. Using in vitro protein analysis, longitudinal fluorescence imaging and cellular, neuronal, and transgenic mouse models, we establish that UBQLN2 is intrinsically prone to self-assemble into higher-order complexes, including liquid-like droplets and amyloid aggregates. UBQLN2 self-assembly and solubility are reciprocally modulated by the protein’s ubiquitin-like and ubiquitin-associated domains. Moreover, a pathogenic UBQLN2 missense mutation impairs droplet dynamics and favors amyloid-like aggregation associated with neurotoxicity. These data emphasize the critical link between UBQLN2’s role in ubiquitin-dependent pathways and its propensity to self-assemble and aggregate in neurodegenerative diseases.

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39

Sastry, M. V. Krishna, and A. Surolia. "Intrinsic fluorescence studies on saccharide binding to Artocarpus integrifolia lectin." Bioscience Reports 6, no. 10 (October 1, 1986): 853–60. http://dx.doi.org/10.1007/bf01116238.

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The combining region of Artocarpus integrifolia lectin has been studied by using the ligand-induced changes in the fluorescence of the lectin. The saccharide binding properties of the lectin show that C-l, C-2, C-4, and C-6 hydroxyl groups of D-galactose are important loci for sugar binding. The α-anorner of galactose binds more strongly than its β-counterpart. Inversion in the configuration at C-4 as in glucose results in a loss of binding to the lectin. The C-6 hydroxyl group is also presumably involved in binding as D-fucose does not bind to the lectin. The lectin binds to the Thomsen-Friedenreich antigen (Galβ(1→3)GalNAc) more strongly than the other disaccharides studied, viz. Gal/β (1→4) Gal and Galβ (1→3) GlcNAc, which are topographically similar to T-antigen. This observation suggests that the combining region of Artocarpus lectin is complementary to that of T-antigen. Solvent accessibility of the protein fluorophores have been probed by the quenching of protein fluorescence by Iodide ion in the absence and presence of sugar. In the presence of sugar a slight inaccessibility of the fluorophores to the solvent has been observed.

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Akiyama, Shuji, Atsushi Mukaiyama, and Takao Kondo. "3D1346 Circadian fluctuation of intrinsic tryptophan fluorescence of cyanobacterial clock protein KaiC(3D Protein: Structure & Function 3,The 49th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 51, supplement (2011): S119. http://dx.doi.org/10.2142/biophys.51.s119_4.

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41

Pedersen, Morten E., Jesper Østergaard, and Henrik Jensen. "Quantification of Structural Integrity and Stability Using Nanograms of Protein by Flow-Induced Dispersion Analysis." Molecules 27, no. 8 (April 13, 2022): 2506. http://dx.doi.org/10.3390/molecules27082506.

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In the development of therapeutic proteins, analytical assessment of structural stability and integrity constitutes an important activity, as protein stability and integrity influence drug efficacy, and ultimately patient safety. Existing analytical methodologies solely rely on relative changes in optical properties such as fluorescence or scattering upon thermal or chemical perturbation. Here, we present an absolute analytical method for assessing protein stability, structure, and unfolding utilizing Taylor dispersion analysis (TDA) and LED-UV fluorescence detection. The developed TDA method measures the change in size (hydrodynamic radius) and intrinsic fluorescence of a protein during in-line denaturation with guanidinium hydrochloride (GuHCl). The conformational stability of the therapeutic antibody adalimumab and human serum albumin were characterized as a function of pH. The simple workflow and low sample consumption (40 ng protein per data point) of the methodology make it ideal for assessing protein characteristics related to stability in early drug development or when having a scarce amount of sample available.

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Caires, Anderson, Luciano Costa, and Joelson Fernandes. "A close analysis of metal-enhanced fluorescence of tryptophan induced by silver nanoparticles: wavelength emission dependence." Open Chemistry 11, no. 1 (January 1, 2013): 111–15. http://dx.doi.org/10.2478/s11532-012-0139-6.

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AbstractIn the last few years, silver nanoparticles have been proposed as a promising alternative for the label-free detection of proteins via metal-enhanced fluorescence. Generally, the aromatic amino acid tryptophan is most frequently used in this type of studies, because the intrinsic fluorescence of proteins is usually dominated by tryptophan emissions. In the present study, we evaluated the fluorescence behavior of tryptophan in the presence of a silver colloid with nanoparticles of 100 nm in diameter. The results showed that a nanoparticles concentration of 32 mg L−1 induced maximum fluorescence enhancement. However, the metal-enhanced fluorescence was dependent on the emission wavelength of tryptophan, and this phenomenon was closely related to the metal surface reabsorption process (inner filter effect), suggesting that the plasmon resonance reabsorption effect should be taken into account in analyses involving protein studies by metal-enhanced fluorescence.

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Ladokhin, A. S., and P. W. Holloway. "Fluorescence of membrane-bound tryptophan octyl ester: a model for studying intrinsic fluorescence of protein-membrane interactions." Biophysical Journal 69, no. 2 (August 1995): 506–17. http://dx.doi.org/10.1016/s0006-3495(95)79924-6.

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44

Tsonev, Latchezar I., and Allen G. Hirsh. "Fluorescence ratio intrinsic basis states analysis: a novel approach to monitor and analyze protein unfolding by fluorescence." Journal of Biochemical and Biophysical Methods 45, no. 1 (August 2000): 1–21. http://dx.doi.org/10.1016/s0165-022x(00)00070-1.

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45

Hlady, V., J. Rickel, and J. D. Andrade. "Fluorescence of adsorbed protein layers. II. Adsorption of human lipoproteins studied by total internal reflection intrinsic fluorescence." Colloids and Surfaces 34, no. 2 (January 1988): 171–83. http://dx.doi.org/10.1016/0166-6622(88)80095-7.

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46

Fonin, Alexander V., Olga V. Stepanenko, Irina M. Kuznetsova, Konstantin K. Turoverov, Elena I. Kostyleva, and Vladimir I. Vorobyev. "Interaction between linker histone H1 and non-histone chromatin protein HMGB1." Spectroscopy 24, no. 1-2 (2010): 165–68. http://dx.doi.org/10.1155/2010/745671.

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The possibility of interaction between linker histone H1 and non-histone chromatin protein HMGB1 was studied by intrinsic UV-fluorescence, far and near-UV CD and light scattering. The obtained data allow us to assume that the increase of histone H1 content in the HMGB1 solutions in a low ionic strength is accompanied by the destruction of HMGB1 associates. The interaction between proteins causes the increase of ordered regions in the protein molecules and the minor changes in their tertiary structure.

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47

Solomaha, Elena, and H. Clive Palfrey. "Conformational changes in dynamin on GTP binding and oligomerization reported by intrinsic and extrinsic fluorescence." Biochemical Journal 391, no. 3 (October 25, 2005): 601–11. http://dx.doi.org/10.1042/bj20050707.

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The effects of guanine nucleotides on the intrinsic and extrinsic fluorescence properties of dynamin were assessed. The intrinsic Trp (tryptophan) fluorescence spectra of purified recombinant dynamin-1 and -2 were very similar, with a maximum at 332 nm. Collisional quenching by KI was weak (∼30%), suggesting that the majority of Trp residues are buried. Binding of guanine nucleotides decreased intrinsic fluorescence by 15–20%. Titration of the effects showed that GTP and GDP bound to a single class of non-interacting sites in dynamin tetramers with apparent dissociation constants (Kd) values of 5.4 and 7.4 μM (dynamin-1) and 13.2 and 7.1 μM (dynamin-2) respectively. Similar dissociation constant values for both nucleotides were obtained by titrating the quenching of IAEDANS [N-iodoacetyl-N′-(5-sulpho-1-naphthyl)ethylenediamine]-labelled dynamin-2. Despite the similar binding affinities, GTP and GDP result in different conformations of the protein, as revealed by sensitivity to proteinase K fragmentation. Dynamins contain five Trp residues, of which four are in the PH domain (pleckstrin homology domain) and one is in the C-terminal PRD (proline/arginine-rich domain). Guanine nucleotides quenched fluorescence emission from a truncated (ΔPRD) mutant dynamin-1 to the same extent as in the full-length protein, suggesting conformational coupling between the G (groove)-domain and the PH domain. Efficient resonance energy transfer from PH domain Trp residues to bound mant-GTP [where mant stands for 2′-(3′)-O-(N-methylanthraniloyl)] suggests that the G-domain and PH domain are in close proximity (5–6 nm). Promotion of dynamin-2 oligomerization, by reduction in ionic strength or increasing protein concentration, had little effect on intrinsic dynamin fluorescence. However, fluorescence emission from IAEDANS·dynamin-2 showed a significant spectral shift on oligomerization. In addition, energy transfer was observed when oligomerization was promoted in mixtures of IAEDANS·dynamin-2 and 4-(4-dimethylaminophenylazo)benzoic acid-coupled dynamin-2, an effect that was counteracted by GTP but not GDP.

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Provenzano, Paolo P., Kevin W. Eliceiri, Long Yan, Aude Ada-Nguema, Matthew W. Conklin, David R. Inman, and Patricia J. Keely. "Nonlinear Optical Imaging of Cellular Processes in Breast Cancer." Microscopy and Microanalysis 14, no. 6 (November 6, 2008): 532–48. http://dx.doi.org/10.1017/s1431927608080884.

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AbstractNonlinear optical imaging techniques such as multiphoton and second harmonic generation (SHG) microscopy used in conjunction with novel signal analysis techniques such as spectroscopic and fluorescence excited state lifetime detection have begun to be used widely for biological studies. This is largely due to their promise to noninvasively monitor the intracellular processes of a cell together with the cell's interaction with its microenvironment. Compared to other optical methods these modalities provide superior depth penetration and viability and have the additional advantage in that they are compatible technologies that can be applied simultaneously. Therefore, application of these nonlinear optical approaches to the study of breast cancer holds particular promise as these techniques can be used to image exogeneous fluorophores such as green fluorescent protein as well as intrinsic signals such as SHG from collagen and endogenous fluorescence from nicotinamide adenine dinucleotide or flavin adenine dinucleotide. In this article the application of multiphoton excitation, SHG, and fluorescence lifetime imaging microscopy to relevant issues regarding the tumor-stromal interaction, cellular metabolism, and cell signaling in breast cancer is described. Furthermore, the ability to record and monitor the intrinsic fluorescence and SHG signals provides a unique tool for researchers to understand key events in cancer progression in its natural context.

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Malekian, Bita, Ivan Maximov, Rainer Timm, Tommy Cedervall, and Dan Hessman. "A Method for Investigation of Size-Dependent Protein Binding to Nanoholes Using Intrinsic Fluorescence of Proteins." ACS Omega 2, no. 8 (August 22, 2017): 4772–78. http://dx.doi.org/10.1021/acsomega.7b00241.

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50

Donato, H., R. S. Mani, and C. M. Kay. "Spectral studies on the cadmium-ion-binding properties of bovine brain S-100b protein." Biochemical Journal 276, no. 1 (May 15, 1991): 13–18. http://dx.doi.org/10.1042/bj2760013.

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The effect of Cd2+ binding on bovine brain S-100b protein was studied using c.d. u.v. difference spectroscopy and fluorescence measurements. At pH 7.5, S-100b protein binds two Cd2+ ions per monomer with a Kd value of 3 x 10(-5) M. Addition of Cd2+ resulted in perturbing the single tyrosine residue (Tyr17) in the protein as indicated by u.v. difference spectroscopy and aromatic c.d. measurements. In the presence of Cd2+, the tyrosine residue moves to a more non-polar environment, since a red shift was observed in the u.v. difference spectrum. When the protein was excited at 278 nm, the tyrosine fluorescence emission maximum was centred at 306 nm. Cd2+ addition resulted in an increase in intrinsic fluorescence intensity. Fluorescence titration with Cd2+ indicated the protein binds Cd2+ with a Kd value of 3 x 10(-5) M. 2-p-Toluidinylnaphthalene-6-sulphonate-labelled protein, when excited at 345 nm, had a fluorescence emission maximum at 440 nm. Addition of Cd2+ to labelled protein resulted in a 5-fold increase in fluorescence intensity accompanied by a 5 nm blue shift in the emission maximum, suggesting that the probe, in the presence of Cd2+, moves to a hydrophobic domain. U.v. difference spectroscopic studies indicated a unique Cd2(+)-binding site on the protein, since Cd2+ addition yielded a large positive absorption band in the 240 nm region that is not found with either Ca2+ or Zn2- ions. Similar absorption bands have been observed in Cd-protein complexes such as Cd-metallothionein [Vasak, Kagi & Hill (1981) Biochemistry 20, 2852-2856] and also in model complexes of Cd2+ with 2-mercaptoethanol. This absorption band is believed to arise as a result of charge-transfer transitions between the thiolate and Cd2+. Of the two Cd2- -binding sites on the beta-chain, one must be located at the N-terminal end near the single tyrosine residue, since Cd2- and Zn2+ produced similar effects on the intrinsic protein fluorescence. The other Cd2+ site which is unique to Cd2+ must be Cys84, located at the C-terminal end.

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