메뉴 건너뛰기




Volumn 15, Issue 12, 2014, Pages 22518-22538

Intrinsic tryptophan fluorescence in the detection and analysis of proteins: A focus on förster resonance energy transfer techniques

Author keywords

Biosensors; FRET; Immunoassay; Intrinsic fluorescence; Label free detection; Protein imaging; Tryptophan fluorescence

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; BOVINE SERUM ALBUMIN; FLUORESCENT DYE; NUCLEOTIDE BINDING PROTEIN; PHENYLALANINE; PROTEIN RET; STREPTAVIDIN; TRYPTOPHAN; TYROSINE; PROTEIN; PROTEOME;

EID: 84937605198     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms151222518     Document Type: Review
Times cited : (692)

References (82)
  • 1
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • Ladokhin, A.S.; Jayasinghe, S.; White, S.H. How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? Anal. Biochem. 2000, 285, 235–245
    • (2000) Anal. Biochem , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 4
    • 34548576414 scopus 로고
    • Extraction, purificationand properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura, O.; Johnson, F.; Saiga, Y. Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell. Comp. Physiol. 1962, 59, 223–239
    • (1962) J. Cell. Comp. Physiol , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.2    Saiga, Y.3
  • 5
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescence protein.
    • Tsien, R.Y. The green fluorescence protein. Annu. Rev. Biochem. 1998, 67, 509–544
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 6
    • 84875871080 scopus 로고    scopus 로고
    • Chemical biology-based approaches on fluorescent labeling of proteins in live cells.
    • Jung, D.; Min, K.; Jung, J.; Jang, W.; Kwon, Y. Chemical biology-based approaches on fluorescent labeling of proteins in live cells. Mol. BioSyst. 2013, 9, 862–872
    • (2013) Mol. Biosyst , vol.9 , pp. 862-872
    • Jung, D.1    Min, K.2    Jung, J.3    Jang, W.4    Kwon, Y.5
  • 7
    • 84906860985 scopus 로고    scopus 로고
    • Smartphone fluorescence spectroscopy.
    • Yu, H.; Tan, Y.; Cunningham, B.T. Smartphone fluorescence spectroscopy. Anal. Chem. 2014, 86, 8805–8813
    • (2014) Anal. Chem , vol.86 , pp. 8805-8813
    • Yu, H.1    Tan, Y.2    Cunningham, B.T.3
  • 8
    • 84901272377 scopus 로고    scopus 로고
    • Studies of protein folding and dynamics using single molecule fluorescence spectroscopy
    • Basak, S.; Chattopadhyay, K. Studies of protein folding and dynamics using single molecule fluorescence spectroscopy. Phys. Chem. Chem. Phys. 2014, 16, 11139–11149
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 11139-11149
    • Basak, S.1    Chattopadhyay, K.2
  • 9
    • 0037022652 scopus 로고    scopus 로고
    • Two-photon excitation microscopy of tryptophan-containing proteins
    • Lippitz, M.; Erker, W.; Decker, H.; van Holde, K.E.; Basché, T. Two-photon excitation microscopy of tryptophan-containing proteins. PNAS 2002, 99, 2772–2777
    • (2002) PNAS , vol.99 , pp. 2772-2777
    • Lippitz, M.1    Erker, W.2    Decker, H.3    Van Holde, K.E.4    Basché, T.5
  • 11
    • 79951963011 scopus 로고    scopus 로고
    • FRET microscopy in 2010: The legacy of Theodor Förster-Resonance-Energy-Transfer on the 100th anniversary of his birth
    • Sun, Y.; Wallrabe, H.; Seo, S.A.; Periasamy, A. FRET microscopy in 2010: The legacy of Theodor Förster-Resonance-Energy-Transfer on the 100th anniversary of his birth. Chemphyschem 2011, 12, 462–474
    • (2011) Chemphyschem , vol.12 , pp. 462-474
    • Sun, Y.1    Wallrabe, H.2    Seo, S.A.3    Periasamy, A.4
  • 12
    • 27144515959 scopus 로고    scopus 로고
    • Cell and tissue autofluorescence research and diagnostic applications
    • Monici, M. Cell and tissue autofluorescence research and diagnostic applications. Biotechnol. Annu. Rev. 2005, 11, 227–256
    • (2005) Biotechnol. Annu. Rev , vol.11 , pp. 227-256
    • Monici, M.1
  • 13
    • 0035871239 scopus 로고    scopus 로고
    • Seeing the wood through the trees: A review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence.
    • Billinton, N.; Knight, A.W. Seeing the wood through the trees: A review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence. Anal. Biochem. 2001, 291, 175–197
    • (2001) Anal. Biochem , vol.291 , pp. 175-197
    • Billinton, N.1    Knight, A.W.2
  • 14
    • 33646918845 scopus 로고    scopus 로고
    • Probing protein folding and conformational transitions with fluorescence
    • Royer, C.A. Probing protein folding and conformational transitions with fluorescence. Chem. Rev. 2006, 106, 1769–1784
    • (2006) Chem. Rev , vol.106 , pp. 1769-1784
    • Royer, C.A.1
  • 15
    • 70449159833 scopus 로고
    • Ultraviolet fluorescence of the aromatic amino acids
    • Teale, F.W.J.; Weber, G. Ultraviolet fluorescence of the aromatic amino acids. Biochem. J. 1957, 65, 476–482
    • (1957) Biochem. J , vol.65 , pp. 476-482
    • Teale, F.1    Weber, G.2
  • 16
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y.; Barkley, M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry 1998, 37, 9976–9982
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 17
    • 0027985340 scopus 로고
    • Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state
    • Swaminathan, R.; Krishnamoorthy, G.; Periasamy, N. Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state. Biophys. J. 1994, 67, 2013–2023
    • (1994) Biophys. J , vol.67 , pp. 2013-2023
    • Swaminathan, R.1    Krishnamoorthy, G.2    Periasamy, N.3
  • 18
    • 0000810656 scopus 로고
    • The tryptophan fluorescence lifetime puzzle. A study of decay times in aqueous solution as a function of pH and buffer composition
    • Gudgin, E.; Lopez-Delgado, R.; Ware, W.R. The tryptophan fluorescence lifetime puzzle. A study of decay times in aqueous solution as a function of pH and buffer composition. Can. J. Chem. 1981, 59, 1037–1044
    • (1981) Can. J. Chem , vol.59 , pp. 1037-1044
    • Gudgin, E.1    Lopez-Delgado, R.2    Ware, W.R.3
  • 19
    • 84894566908 scopus 로고    scopus 로고
    • Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution
    • Albani, J. Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution. J. Fluoresc. 2014, 24, 93–104
    • (2014) J. Fluoresc , vol.24 , pp. 93-104
    • Albani, J.1
  • 20
    • 84894542412 scopus 로고    scopus 로고
    • Origin of tryptophan fluorescence lifetimes. Part 2: Fluorescence lifetimes origin of tryptophan in proteins
    • Albani, J. Origin of tryptophan fluorescence lifetimes. Part 2: Fluorescence lifetimes origin of tryptophan in proteins. J. Fluoresc. 2014, 24, 105–117
    • (2014) J. Fluoresc , vol.24 , pp. 105-117
    • Albani, J.1
  • 22
    • 0028965143 scopus 로고
    • Stark effect spectroscopy of tryptophan
    • Pierce, D.; Boxer, S. Stark effect spectroscopy of tryptophan. Biophys. J. 1995, 68, 1583–1591
    • (1995) Biophys. J , vol.68 , pp. 1583-1591
    • Pierce, D.1    Boxer, S.2
  • 23
    • 0001516275 scopus 로고
    • The ultraviolet fluorescence of proteins in neutral solution
    • Teale, F.W.J. The ultraviolet fluorescence of proteins in neutral solution. Biochem. J. 1960, 72, 381–388
    • (1960) Biochem. J , vol.72 , pp. 381-388
    • Teale, F.1
  • 24
    • 0024202514 scopus 로고
    • Lifetime distributions and anisotropy decays of indole fluorescence in cyclohexane/ethanol mixtures by frequency-domain fluorometry
    • Gryczynski, I.; Wiczk, W.; Johnson, M.L.; Lakowicz, J.R. Lifetime distributions and anisotropy decays of indole fluorescence in cyclohexane/ethanol mixtures by frequency-domain fluorometry. Biophys. Chem. 1988, 32, 173–185
    • (1988) Biophys. Chem , vol.32 , pp. 173-185
    • Gryczynski, I.1    Wiczk, W.2    Johnson, M.L.3    Lakowicz, J.R.4
  • 27
    • 0020730977 scopus 로고
    • Conformational heterogeneity of the copper binding site in azurin. A time-resolved fluorescence study
    • Szabo, A.; Stepanik, T.; Wayner, D.; Young, N. Conformational heterogeneity of the copper binding site in azurin. A time-resolved fluorescence study. Biophys. J. 1983, 41, 233–244
    • (1983) Biophys. J. , vol.41 , pp. 233-244
    • Szabo, A.1    Stepanik, T.2    Wayner, D.3    Young, N.4
  • 28
    • 0025929570 scopus 로고    scopus 로고
    • Fluorescence techniques for studying protein structure
    • John Wiley & Sons, Inc.: Hoboken, NJ, USA
    • Eftink, M.R. Fluorescence techniques for studying protein structure. In Methods of Biochemical Analysis; John Wiley & Sons, Inc.: Hoboken, NJ, USA, 2006; pp. 127–205
    • (2006) Methods of Biochemical Analysis , pp. 127-205
    • Eftink, M.R.1
  • 29
    • 0037450579 scopus 로고    scopus 로고
    • Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone
    • Callis, P.R.; Vivian, J.T. Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone. Chem. Phys. Lett. 2003, 369, 409–414
    • (2003) Chem. Phys. Lett , vol.369 , pp. 409-414
    • Callis, P.R.1    Vivian, J.T.2
  • 30
    • 0014633510 scopus 로고
    • The interaction of the ground and excited states of indole derivatives with electron scavengers
    • Steiner, R.; Kirby, E. The interaction of the ground and excited states of indole derivatives with electron scavengers. J. Phys. Chem. 1969, 73, 4130–4135
    • (1969) J. Phys. Chem , vol.73 , pp. 4130-4135
    • Steiner, R.1    Kirby, E.2
  • 31
    • 0029904741 scopus 로고    scopus 로고
    • The peptide bond quenches indole fluorescence
    • Chen, Y.; Liu, B.; Yu, H.T.; Barkley, M. The peptide bond quenches indole fluorescence. J. Am. Chem. Soc. 1996, 118, 9271–9278
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 9271-9278
    • Chen, Y.1    Liu, B.2    Yu, H.T.3    Barkley, M.4
  • 32
    • 0037036745 scopus 로고    scopus 로고
    • Intramolecular quenching of tryptophan fluorescence by the peptide bond in cyclic hexapeptides
    • Adams, P.; Chen, Y.; Ma, K.; Zagorski, M.; Sönnichsen, F.; McLaughlin, M.; Barkley, M. Intramolecular quenching of tryptophan fluorescence by the peptide bond in cyclic hexapeptides. J. Am. Chem. Soc. 2002, 124, 9278–9286
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 9278-9286
    • Adams, P.1    Chen, Y.2    Ma, K.3    Zagorski, M.4    Sönnichsen, F.5    McLaughlin, M.6    Barkley, M.7
  • 35
    • 84869161564 scopus 로고    scopus 로고
    • Tryptophan rotamer distribution revealed for the alpha-helix in tear lipocalin by site-directed tryptophan fluorescence
    • Gasymov, O.K.; Abduragimov, A.R.; Glasgow, B.J. Tryptophan rotamer distribution revealed for the alpha-helix in tear lipocalin by site-directed tryptophan fluorescence. J. Phys. Chem. B 2012, 116, 13381–13388
    • (2012) J. Phys. Chem. B , vol.116 , pp. 13381-13388
    • Gasymov, O.K.1    Abduragimov, A.R.2    Glasgow, B.J.3
  • 36
    • 84906495103 scopus 로고    scopus 로고
    • Interaction of cyclodextrins with human and bovine serum albumins: A combined spectroscopic and computational investigation
    • Ghosh, S.; Paul, B.K.; Chattopadhyay, N. Interaction of cyclodextrins with human and bovine serum albumins: A combined spectroscopic and computational investigation. J. Chem. Sci. 2014, 126, 931–944
    • (2014) J. Chem. Sci. , vol.126 , pp. 931-944
    • Ghosh, S.1    Paul, B.K.2    Chattopadhyay, N.3
  • 37
    • 84858155181 scopus 로고    scopus 로고
    • Tryptophan dynamics in the exploration of micro-conformational changes of refolded beta-lactoglobulin after thermal exposure: A steady state and time-resolved fluorescence approach
    • Halder, U.C.; Chakraborty, J.; Das, N.; Bose, S. Tryptophan dynamics in the exploration of micro-conformational changes of refolded beta-lactoglobulin after thermal exposure: A steady state and time-resolved fluorescence approach. J. Photochem. Photobiol. B 2012, 109, 50–57
    • (2012) J. Photochem. Photobiol. B , vol.109 , pp. 50-57
    • Halder, U.C.1    Chakraborty, J.2    Das, N.3    Bose, S.4
  • 38
    • 84879686733 scopus 로고    scopus 로고
    • Fluorescence anisotropy of tyrosinate anion using one-, two- and three-photon excitation
    • Kierdaszuk, B. Fluorescence anisotropy of tyrosinate anion using one-, two- and three-photon excitation. J. Fluoresc. 2013, 23, 339–347
    • (2013) J. Fluoresc , vol.23 , pp. 339-347
    • Kierdaszuk, B.1
  • 39
    • 84871351225 scopus 로고    scopus 로고
    • Comparative study of the fatty acid binding process of a new FABP from cherax quadricarinatus by fluorescence intensity, lifetime and anisotropy
    • Li, J.; Henry, E.; Wang, L.; Delelis, O.; Wang, H.; Simon, F.; Tauc, P.; Brochon, J.C.; Zhao, Y.; Deprez, E. Comparative study of the fatty acid binding process of a new FABP from cherax quadricarinatus by fluorescence intensity, lifetime and anisotropy. PLoS One 2012, 7, e51079
    • (2012) Plos One , vol.7
    • Li, J.1    Henry, E.2    Wang, L.3    Delelis, O.4    Wang, H.5    Simon, F.6    Tauc, P.7    Brochon, J.C.8    Zhao, Y.9    Deprez, E.10
  • 40
    • 84876132765 scopus 로고    scopus 로고
    • A comparative study of interaction of tetracycline with several proteins using time resolved anisotropy, phosphorescence, docking and FRET
    • Mukherjee, M.; Sardar, P.S.; Ghorai, S.K.; Samanta, S.K.; Roy, A.S.; Dasgupta, S.; Ghosh, S. A comparative study of interaction of tetracycline with several proteins using time resolved anisotropy, phosphorescence, docking and FRET. PLoS One 2013, 8, e60940
    • (2013) Plos One , vol.8
    • Mukherjee, M.1    Sardar, P.S.2    Ghorai, S.K.3    Samanta, S.K.4    Roy, A.S.5    Dasgupta, S.6    Ghosh, S.7
  • 41
    • 84884573671 scopus 로고    scopus 로고
    • Binding of antioxidant flavonol morin to the native state of bovine serum albumin: Effects of urea and metal ions on the binding
    • Roy, A.S.; Dinda, A.K.; Chaudhury, S.; Dasgupta, S. Binding of antioxidant flavonol morin to the native state of bovine serum albumin: Effects of urea and metal ions on the binding. J. Lumin. 2014, 145, 741–751
    • (2014) J. Lumin , vol.145 , pp. 741-751
    • Roy, A.S.1    Dinda, A.K.2    Chaudhury, S.3    Dasgupta, S.4
  • 42
    • 84887883766 scopus 로고    scopus 로고
    • Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state
    • Sarkar, S.S.; Udgaonkar, J.B.; Krishnamoorthy, G. Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state. Biophys. J. 2013, 105, 2392–2402
    • (2013) Biophys. J , vol.105 , pp. 2392-2402
    • Sarkar, S.S.1    Udgaonkar, J.B.2    Krishnamoorthy, G.3
  • 44
    • 84886951215 scopus 로고    scopus 로고
    • Etiology of Alzheimer’s disease: Kinetic, thermodynamic and fluorimetric analyses of interactions of pseudo A-peptides with neuronal nitric oxide synthase
    • Padayachee, E.; Whiteley, C. Etiology of Alzheimer’s disease: Kinetic, thermodynamic and fluorimetric analyses of interactions of pseudo A-peptides with neuronal nitric oxide synthase. Neuropeptides 2013, 47, 321–327
    • (2013) Neuropeptides , vol.47 , pp. 321-327
    • Padayachee, E.1    Whiteley, C.2
  • 45
    • 84902776727 scopus 로고    scopus 로고
    • Fluorometric titration approach for calibration of quantity of binding site of purified monoclonal antibody recognizing epitope/hapten nonfluorescent at 340 nm.
    • Yang, X.; Hu, X.; Xu, B.; Wang, X.; Qin, J.; He, C.; Xie, Y.; Li, Y.; Liu, L.; Liao, F. Fluorometric titration approach for calibration of quantity of binding site of purified monoclonal antibody recognizing epitope/hapten nonfluorescent at 340 nm. Anal. Chem. 2014, 86, 5667–5672
    • (2014) Anal. Chem , vol.86 , pp. 5667-5672
    • Yang, X.1    Hu, X.2    Xu, B.3    Wang, X.4    Qin, J.5    He, C.6    Xie, Y.7    Li, Y.8    Liu, L.9    Liao, F.10
  • 46
    • 84894104739 scopus 로고    scopus 로고
    • Spectroscopic study on the interaction between p-nitrophenol and bovine serum albumin
    • Guo, X.; Li, X.; Jiang, Y.; Wu, Q.; Chang, H.; Diao, X.; Sun, Y.; Pan, X.; Zhou, N. A spectroscopic study on the interaction between p-nitrophenol and bovine serum albumin. J. Lumin. 2014, 149, 353–360
    • (2014) J. Lumin. , vol.149 , pp. 353-360
    • Guo, X.1    Li, X.2    Jiang, Y.3    Wu, Q.4    Chang, H.5    Diao, X.6    Sun, Y.7    Pan, X.8    Zhou, N.A.9
  • 47
    • 84894514957 scopus 로고    scopus 로고
    • Investigation on the interaction of pyrene with bovine serum albumin using spectroscopic methods
    • Xu, C.; Gu, J.; Ma, X.; Dong, T.; Meng, X. Investigation on the interaction of pyrene with bovine serum albumin using spectroscopic methods. Spectrochim. Acta A 2014, 125, 391–395
    • (2014) Spectrochim. Acta A , vol.125 , pp. 391-395
    • Xu, C.1    Gu, J.2    Ma, X.3    Dong, T.4    Meng, X.5
  • 48
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • Van de Weert, M.; Stella, L. Fluorescence quenching and ligand binding: A critical discussion of a popular methodology. J. Mol. Struct. 2011, 998, 144–150
    • (2011) J. Mol. Struct , vol.998 , pp. 144-150
    • Van De Weert, M.1    Stella, L.2
  • 49
    • 84855849163 scopus 로고    scopus 로고
    • Fluorescence quenching of tryptophan and tryptophanyl dipeptides in solution
    • Osysko, A.P.; Muíño, P.L. Fluorescence quenching of tryptophan and tryptophanyl dipeptides in solution. J. Biophys. Chem. 2011, 2, 316–321
    • (2011) J. Biophys. Chem. , vol.2 , pp. 316-321
    • Osysko, A.P.1    Muíño, P.L.2
  • 51
    • 0024293340 scopus 로고
    • Structure of azurin from Alcaligenes denitrificans refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules
    • Baker, E.N. Structure of azurin from Alcaligenes denitrificans refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules. J. Mol. Biol. 1988, 203, 1071–1095
    • (1988) J. Mol. Biol , vol.203 , pp. 1071-1095
    • Baker, E.N.1
  • 53
    • 0023043203 scopus 로고
    • Properties of paracoccus denitrificans amicyanin
    • Husain, M.; Davidson, V.L.; Smith, A.J. Properties of paracoccus denitrificans amicyanin. Biochemistry 1986, 25, 2431–2436
    • (1986) Biochemistry , vol.25 , pp. 2431-2436
    • Husain, M.1    Davidson, V.L.2    Smith, A.J.3
  • 54
    • 56449085388 scopus 로고    scopus 로고
    • Optical investigation of the electron transfer protein azurin-gold nanoparticle system.
    • Delfino, I.; Cannistraro, S. Optical investigation of the electron transfer protein azurin-gold nanoparticle system. Biophys. Chem. 2009, 139, 1–7
    • (2009) Biophys. Chem , vol.139 , pp. 1-7
    • Delfino, I.1    Cannistraro, S.2
  • 55
    • 84899548383 scopus 로고    scopus 로고
    • The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site.
    • Dow, B.A.; Sukumar, N.; Matos, J.O.; Choi, M.; Schulte, A.; Tatulian, S.A.; Davidson, V.L. The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site. Arch. Biochem. Biophys. 2014, 550, 20–27
    • (2014) Arch. Biochem. Biophys , vol.550 , pp. 20-27
    • Dow, B.A.1    Sukumar, N.2    Matos, J.O.3    Choi, M.4    Schulte, A.5    Tatulian, S.A.6    Davidson, V.L.7
  • 56
    • 84904021081 scopus 로고    scopus 로고
    • Affinity to bovine serum albumin and anticancer activity of some new water-soluble metal Schiff base complexes
    • Asadi, M.; Asadi, Z.; Zarei, L.; Sadi, S.B.; Amirghofran, Z. Affinity to bovine serum albumin and anticancer activity of some new water-soluble metal Schiff base complexes. Spectrochim. Acta A 2014, 133, 697–706
    • (2014) Spectrochim. Acta A , vol.133 , pp. 697-706
    • Asadi, M.1    Asadi, Z.2    Zarei, L.3    Sadi, S.B.4    Amirghofran, Z.5
  • 58
    • 84906827493 scopus 로고    scopus 로고
    • Fluorescence quenching of (dimethylamino)naphthalene dyes badan and prodan by tryptophan in cytochromes P450 and micelles
    • Pospisil, P.; Luxem, K.E.; Ener, M.; Sykora, J.; Kocabova, J.; Gray, H.B.; Vlcek, A., Jr.; Hof, M. Fluorescence quenching of (dimethylamino)naphthalene dyes badan and prodan by tryptophan in cytochromes P450 and micelles. J. Phys. Chem. B 2014, 118, 10085–10091
    • (2014) J. Phys. Chem. B , vol.118 , pp. 10085-10091
    • Pospisil, P.1    Luxem, K.E.2    Ener, M.3    Sykora, J.4    Kocabova, J.5    Gray, H.B.6    Vlcek, A.7    Hof, M.8
  • 59
    • 84906836864 scopus 로고    scopus 로고
    • Fluorescence quenching studies of gamma-butyrolactone binding protein (CprB) from streptomyces coelicolor A3(2)
    • Biswas, A.; Swarnkar, R.K.; Hussain, B.; Sahoo, S.K.; Pradeepkumar, P.I.; Patwari, G.N.; Anand, R. Fluorescence quenching studies of gamma-butyrolactone binding protein (CprB) from streptomyces coelicolor A3(2). J. Phys. Chem. B 2014, 118, 10035–10042
    • (2014) J. Phys. Chem. B , vol.118 , pp. 10035-10042
    • Biswas, A.1    Swarnkar, R.K.2    Hussain, B.3    Sahoo, S.K.4    Pradeepkumar, P.I.5    Patwari, G.N.6    Anand, R.7
  • 60
    • 84906046797 scopus 로고    scopus 로고
    • Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: Refined analysis by tryptophan fluorescence measurement
    • Michalek, M.; Aisenbrey, C.; Bechinger, B. Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: Refined analysis by tryptophan fluorescence measurement. Eur. Biophys. J. Biophy. 2014, 43, 347–360
    • (2014) Eur. Biophys. J. Biophy. , vol.43 , pp. 347-360
    • Michalek, M.1    Aisenbrey, C.2    Bechinger, B.3
  • 61
    • 84903955016 scopus 로고    scopus 로고
    • Study on the interaction between amphiphilic drug and bovine serum albumin: A thermodynamic and spectroscopic description
    • Rub, M.A.; Khan, J.M.; Asiri, A.M.; Khan, R.H.; ud Din, K. Study on the interaction between amphiphilic drug and bovine serum albumin: A thermodynamic and spectroscopic description. J. Lumin. 2014, 155, 39–46
    • (2014) J. Lumin , vol.155 , pp. 39-46
    • Rub, M.A.1    Khan, J.M.2    Asiri, A.M.3    Khan, R.H.4    Din, U.5
  • 63
    • 84907363983 scopus 로고    scopus 로고
    • Denaturation of bovine serum albumin initiated by sodium dodecyl sulfate as monitored via the intrinsic fluorescence of the protein. Russ
    • Vlasova, I.M.; Zhuravleva, V.V.; Saletsky, A.M. Denaturation of bovine serum albumin initiated by sodium dodecyl sulfate as monitored via the intrinsic fluorescence of the protein. Russ. J. Phys. Chem. B 2014, 8, 385–390
    • (2014) J. Phys. Chem. B , vol.8 , pp. 385-390
    • Vlasova, I.M.1    Zhuravleva, V.V.2    Saletsky, A.M.3
  • 64
    • 80053162595 scopus 로고    scopus 로고
    • Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaA
    • Kozachkov, L.; Padan, E. Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaA. PNAS 2011, 108, 15769–15774
    • (2011) PNAS , vol.108 , pp. 15769-15774
    • Kozachkov, L.1    Padan, E.2
  • 66
    • 84879643394 scopus 로고    scopus 로고
    • Investigation of tryptophan-NADH interactions in live human cells using three-photon fluorescence lifetime imaging and Forster resonance energy transfer microscopy
    • Jyothikumar, V.; Sun, Y.; Periasamy, A. Investigation of tryptophan-NADH interactions in live human cells using three-photon fluorescence lifetime imaging and Forster resonance energy transfer microscopy. J. Biomed. Opt. 2013, 18, 060501
    • (2013) J. Biomed. Opt , vol.18
    • Jyothikumar, V.1    Sun, Y.2    Periasamy, A.3
  • 67
    • 84871653908 scopus 로고    scopus 로고
    • Immunoassay for the detection of mycotoxins that utilizes quenching of the intrinsic fluorescence of antibodies
    • Li, T.; Byun, J.Y.; Kim, B.B.; Shin, Y.B.; Kim, M.G. Label-free homogeneous FRET immunoassay for the detection of mycotoxins that utilizes quenching of the intrinsic fluorescence of antibodies. Biosens. Bioelectron. 2013, 42, 403–408
    • (2013) Biosens. Bioelectron , vol.42 , pp. 403-408
    • Li, T.1    Byun, J.Y.2    Kim, B.B.3    Shin, Y.B.4    Kim, M.G.5    Label-Free Homogeneous, F.6
  • 68
    • 84861830204 scopus 로고    scopus 로고
    • Selective fluorescence resonance energy transfer from serum albumins to a bio-active 3-pyrazolyl-2-pyrazoline derivative: A spectroscopic analysis
    • Sarkar, A.; Bhattacharya, S.C. Selective fluorescence resonance energy transfer from serum albumins to a bio-active 3-pyrazolyl-2-pyrazoline derivative: A spectroscopic analysis. J. Lumin. 2012, 132, 2612–2618
    • (2012) J. Lumin , vol.132 , pp. 2612-2618
    • Sarkar, A.1    Bhattacharya, S.C.2
  • 70
    • 0028924992 scopus 로고
    • Fluorescence resonance energy transfer
    • Clegg, R.M. Fluorescence resonance energy transfer. Curr. Opin. Biotechnol. 1995, 6, 103–110
    • (1995) Curr. Opin. Biotechnol , vol.6 , pp. 103-110
    • Clegg, R.M.1
  • 71
    • 0033030609 scopus 로고    scopus 로고
    • Terbium and rhodamine as labels in a homogeneous time-resolved fluorometric energy transfer assay of the  subunit of human chorionic gonadotropin in gerum
    • Blomberg, K.; Hurskainen, P.; Hemmilä, I. Terbium and rhodamine as labels in a homogeneous time-resolved fluorometric energy transfer assay of the  subunit of human chorionic gonadotropin in gerum. Clin. Chem. 1999, 45, 855–861
    • (1999) Clin. Chem , vol.45 , pp. 855-861
    • Blomberg, K.1    Hurskainen, P.2    Hemmilä, I.3
  • 72
    • 33745667285 scopus 로고    scopus 로고
    • Distance distributions of short polypeptides recovered by fluorescence resonance energy transfer in the 10 Å domain
    • Sahoo, H.; Roccatano, D.; Zacharias, M.; Nau, W.M. Distance distributions of short polypeptides recovered by fluorescence resonance energy transfer in the 10 Å domain. J. Am. Chem. Soc. 2006, 128, 8118–8119
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 8118-8119
    • Sahoo, H.1    Roccatano, D.2    Zacharias, M.3    Nau, W.M.4
  • 73
    • 34548299086 scopus 로고    scopus 로고
    • Tryptophan-to-dye fluorescence energy transfer applied to oxygen sensing by using type-3 copper proteins
    • Zauner, G.; Lonardi, E.; Bubacco, L.; Aartsma, T.J.; Canters, G.W.; Tepper, A.W.J.W. Tryptophan-to-dye fluorescence energy transfer applied to oxygen sensing by using type-3 copper proteins. Chem-Eur. J. 2007, 13, 7085–7090
    • (2007) Chem-Eur. J , vol.13 , pp. 7085-7090
    • Zauner, G.1    Lonardi, E.2    Bubacco, L.3    Aartsma, T.J.4    Canters, G.W.5    Tepper, A.6
  • 74
    • 81555200658 scopus 로고    scopus 로고
    • Multidonor deep-UV FRET study of protein-ligand binding and its potential to obtain structure information
    • Li, Q.; Seeger, S. Multidonor deep-UV FRET study of protein-ligand binding and its potential to obtain structure information. J. Phys. Chem. B 2011, 115, 13643–13649
    • (2011) J. Phys. Chem. B , vol.115 , pp. 13643-13649
    • Li, Q.1    Seeger, S.2
  • 75
    • 68049142975 scopus 로고    scopus 로고
    • Homogeneous noncompetitive assay of protein via Förster-resonance-energy-transfer with tryptophan residue(s) as intrinsic donor(s) and fluorescent ligand as acceptor
    • Liao, F.; Xie, Y.; Yang, X.; Deng, P.; Chen, Y.; Xie, G.; Zhu, S.; Liu, B.; Yuan, H.; Liao, J. Homogeneous noncompetitive assay of protein via Förster-resonance-energy-transfer with tryptophan residue(s) as intrinsic donor(s) and fluorescent ligand as acceptor. Biosens. Bioelectron. 2009, 25, 112–117
    • (2009) Biosens. Bioelectron. , vol.25 , pp. 112-117
    • Liao, F.1    Xie, Y.2    Yang, X.3    Deng, P.4    Chen, Y.5    Xie, G.6    Zhu, S.7    Liu, B.8    Yuan, H.9    Liao, J.10
  • 76
    • 77956072696 scopus 로고    scopus 로고
    • Fluorescent ribonucleoside as a FRET acceptor for tryptophan in native proteins
    • Xie, Y.; Maxson, T.; Tor, Y. Fluorescent ribonucleoside as a FRET acceptor for tryptophan in native proteins. J. Am. Chem. Soc. 2010, 132, 11896–11897
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 11896-11897
    • Xie, Y.1    Maxson, T.2    Tor, Y.3
  • 77
    • 84889058081 scopus 로고    scopus 로고
    • Discovery of coumarin derivatives as fluorescence acceptors for intrinsic fluorescence resonance energy transfer of proteins
    • Kim, J.H.; Sumranjit, J.; Kang, H.J.; Chung, S.J. Discovery of coumarin derivatives as fluorescence acceptors for intrinsic fluorescence resonance energy transfer of proteins. Mol. BioSyst. 2014, 10, 30–33
    • (2014) Mol. Biosyst , vol.10 , pp. 30-33
    • Kim, J.H.1    Sumranjit, J.2    Kang, H.J.3    Chung, S.J.4
  • 78
    • 0025327759 scopus 로고
    • Studies on the biotin-binding sites of avidin and streptavidin tyrosine residues are involved in the binding site
    • Gitlin, G.; Bayer, E.A.; Wilchek, M. Studies on the biotin-binding sites of avidin and streptavidin tyrosine residues are involved in the binding site. Biochem. J. 1990, 269, 517–530
    • (1990) Biochem. J. , vol.269 , pp. 517-530
    • Gitlin, G.1    Bayer, E.A.2    Wilchek, M.3
  • 79
    • 84873124587 scopus 로고    scopus 로고
    • Comparison of Förster-resonance-energy-transfer acceptors for tryptophan and tyrosine residues in native proteins as donors
    • Zhang, Y.; Yang, X.; Liu, L.; Huang, Z.; Pu, J.; Long, G.; Zhang, L.; Liu, D.; Xu, B.; Liao, J. Comparison of Förster-resonance-energy-transfer acceptors for tryptophan and tyrosine residues in native proteins as donors. J. Fluoresc. 2013, 23, 147–157
    • (2013) J. Fluoresc. , vol.23 , pp. 147-157
    • Zhang, Y.1    Yang, X.2    Liu, L.3    Huang, Z.4    Pu, J.5    Long, G.6    Zhang, L.7    Liu, D.8    Xu, B.9    Liao, J.10
  • 80
    • 84901064788 scopus 로고    scopus 로고
    • Selective and sensitive homogenous assay of serum albumin with 1-anilinonaphthalene-8-sulphonate as a biosensor
    • Qin, J.; Li, Y.; He, C.; Yang, X.; Xie, Y.; Hu, X.; Chen, C.; Wang, L.; Pu, J.; Liao, F. Selective and sensitive homogenous assay of serum albumin with 1-anilinonaphthalene-8-sulphonate as a biosensor. Anal. Chim. Acta 2014, 829, 60–67
    • (2014) Anal. Chim. Acta , vol.829 , pp. 60-67
    • Qin, J.1    Li, Y.2    He, C.3    Yang, X.4    Xie, Y.5    Hu, X.6    Chen, C.7    Wang, L.8    Pu, J.9    Liao, F.10
  • 81
    • 0025343040 scopus 로고
    • Use of 1-anilino-8-naphthalene sulfonate as a fluorescent probe in the investigation of drug interactions with human alpha-1-acid glycoprotein and serum albumin
    • Essassi, D.; Zini, R.; Tillement, J.P. Use of 1-anilino-8-naphthalene sulfonate as a fluorescent probe in the investigation of drug interactions with human alpha-1-acid glycoprotein and serum albumin. J. Pharm. Sci. 1990, 79, 9–13
    • (1990) J. Pharm. Sci. , vol.79 , pp. 9-13
    • Essassi, D.1    Zini, R.2    Tillement, J.P.3
  • 82
    • 70249089273 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of the interaction of 1-anilino-naphthalene-8-sulfonate with proteins
    • Cattoni, D.I.; Kaufman, S.B.; Flecha, F.L.G. Kinetics and thermodynamics of the interaction of 1-anilino-naphthalene-8-sulfonate with proteins. Biochim. Biophys. Acta Proteins Proteomics 2009, 1794, 1700–1708.
    • (2009) Biochim. Biophys. Acta Proteins Proteomics , vol.1794 , pp. 1700-1708
    • Cattoni, D.I.1    Kaufman, S.B.2    Flecha, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.