Structure and Dynamics of Macromolecules: Absorption and Fluorescence Studies

Structure and Dynamics of Macromolecules: Absorption and Fluorescence Studies

Volumn , Issue , 2004, Pages 1-414

  Albani, J R ^a  

^a UNIV LILLE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMICS; FLUORESCENCE SPECTROSCOPY; MACROMOLECULES;

ABSORPTION AND FLUORESCENCE SPECTROSCOPY; FLUORESCENCE STUDIES; GOVERNMENT LABORATORIES; INSTITUTIONAL LIBRARIES; STRUCTURE AND DYNAMICS;

FLUORESCENCE;

EID: 33745444045     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-444-51449-3.X5000-X     Document Type: Book

References (342)

1. Ackroyd R., Kelty C., Brown N., Reed M. The history of photodetection and photodynamic therapy. Photochemistry and Photobiology 2001, 74:656-669.
2. Alcala J.R., Gratton E., Jameson D.M. A multifrequency phase fluorometer using the harmonic content of a mode-locked laser. Analytical Instrumentation 1985, 14:225-240.
3. Albani J. Fluorescence studies on the interaction between two cytochromes extracted from the yeast, Hansenula anomala. Archives of Biochemistry and Biophysics 1985, 243:292-297.
4. Albani J., Alpert B., Krajcarski D., Szabo A.G. A fluorescence decay time study of tryptophan in isolated hemoglobin subunits. FEBS Letters 1985, 182:302-304.
5. Albani J., Alpert B. Porphyrin motions in the myoglobin heme-pocket. Chemical Physical Letters. 1986, 131:147-152.
6. Albani J., Alpert B. Fluctuation domains in myoglobin. Fluorescence quenching studies. European Journal of Biochemistry 1987, 162:175-178.
7. 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and polarization of 2-p-toluidinylnaphthalene-6-sulfonate (TNS and of tryptophan residues. Biophysical Chemistry 1992, 44:129-137.
8. Albani J. A study of the interaction between two proteins, one containing a flavin mononucleotide. Journal of Biochemical and Biophysical Methods 1993, 26:105-112.
9. Albani J.R. Effect of sialic acids and ß-drug adrenergic blocker, propranolol, on dynamics of human alpha 1 acid glycoprotein. A fluorescence study. J. Biochem. 1994, 116:625-630.
10. 1-acid glycoprotein (orosomucoid) and 2-p-toluidinylnaphthaalene-6-sulfonate. Photochemistry and Photobiology 1995, 62:30-34.
11. Albani J.R. Dynamics of Lens culinaris agglutinin studied by red-edge excitation spectra and anisotropy measurements of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues. Journal of fluorescence 1996, 6:199-208.
12. 1-acid glycoprotein. Biochimica Biophysica Acta. 1996, 1291:215-220.
13. 1-acid glycoprotein. Biochimica Biophysica Acta 1997, 1336:349-359.
14. 2 core and flavodehydrogenase from the yeast Hansenual anomala. Photochem. Photobiol. 1997, 66:72-75.
15. Albani J.R., Debray H., Vincent M., Gallay J. Role of the carbohydrate moiety and of the alpha L-fucose in the stabilization and the dynamics of the Lens culinaris agglutinin-glycoprotein complex. A fluorescence study. Journal of Fluorescence 1997, 7:293-298.
16. Albani J.R. Lens culinaris agglutinin - lactotransferrin and serotransferrin complexes, folwed by fluorescence intensity quenching of fluorescein (FITC) with iodide and temperature. Biochimica Biophysica Acta 1998, 1425:405-410.
17. 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra. Journal of Fluorescence 1998, 8:213-224.
18. 1-acid glycoprotein (orosomucoid): a fluorescence approach. Spectrochimica Acta Part A 1998, 54:175-183.
19. 1-acid glycoprotein. Carbohydrate Research 1998, 314:169-175. 1999.
20. 1-acid glycoprotein. Carbohydrate Research 1998 and 1999, 318:194-200.
21. 1-acid glycoprotein (orosomucoid). Quenching resolved emission anisotropy studies. Spectrochimica Acta, Part A 1999, 55:2353-2360.
22. 1-acid glycoprotein (orosumucoid) followed by red-edge excitation spectra and emission anisotropy studies of Calcofluor White. Carbohydrate Research 1999, 322:87-94.
23. 1-acid glycoprotein (orosomucoid) and saturating concentrations of Calcofluor White. A fluorescence study. Carbohydrate Research 2000, 327:333-340.
24. 1-acid glycoprotein (orosomucoid) on the structure and dynamics of the protein moiety. A fluorescence study. Carbohydrate Research 2001, 334:141-151.
25. Albani J.R. Absorption et Fluorescence: Principes et Applications 2001, Editions Lavoisier-Tec & Doc., Paris.
26. 1-acid glycoprotein (orosomucoid) and progesterone. A fluorescence study. Carbohydrate Research 2002, 337:1405-1410.
27. 1-acid glycoprotein (orosomucoid) and the fluorescence of the protein. Carbohydrate Research 2003, 338:1097-1101.
28. 1-acid glycoprotein (rosomucoid) and the glycosylation site of the protein. Carbohydrate Research 2003, 338:2233-2236.
29. Albani J.R., Demuynck S., Grumiaux F., Leprêtre A. Fluorescence fingerprints of Eisenia fetida and Eisenia andrei. Photochemistry and Photobiology 2003, 78:599-602.
30. 1-acid glycoprotein (orosomucoid). Straightforward fluorescence experiments revealing the presence of a binding pocket. Carbohysrate Research 2004, 339:607-612.
31. 1-acid glycoprotein (orosomucoid) on the local dynamics of Trp residues. Chemistry & Biodiversity 2004, 1:152-160.
32. Alpert B., Lopez-Delgado R Fluorescence lifetimes of haem proteins excited Into the tryptophan absorption band with synchrotron radiation. Nature 1976, 263:445-446.
33. *1,*2. Carbohydrate Research 1981, 95:263-282.
34. Amisha Kamal, J. K. and Behere, D. V. Steady-state and picosecond time-resolved fluorescence studies on native and apo seed coat soybean peroxidase. Biochemical Biophysical Research Communication 289, 427-433.
35. Andersen K.V., Poulsen F.M. The three-dimensional structure of acylcoenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy. Journal of Biomolecular NMR 1993, 3:271-284.
36. André F Contribution à l'analyse expérimentale de la reproduction des lombriciens. Bulletin Biologique de la France et de la Belgique 1963, 97:3-101.
37. Athes V., Lange R., Combes D. Influence of polyols on the structural properties of Kluyveromyces lactis beta-galactosidase under high hydrostatic pressure. European Journal of Biochemistry 1998, 255:206-212.
38. Badea M.G., Brand L. Time-resolved fluorescence measurements. Methods in Enzymology 1979, 61:378-425.
39. Baker E.N., Lindley P.F. New perspectives on the structure and function of transferrins. Journal of Inorganic Biochemistry 1992, 47:147-160.
40. Balabanli B., Kamisaki Y., Martin E., Murad F. Requirements for heme and thiols for the nonenzymatic modification of nitrotyrosine. Proceedings of the Natural Academy of Sciences. U.S.A. 1999, 96:13136-13141.
41. 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 1992, 31:5269-5278.
42. Barik A., Priyadarsini K.I., Mohan H. Photophysical Studies on Binding of Curcumin to Bovine Serum Albumin. Photochemistry and Photobiology 2003, 77:597-603.
43. Barrick D., Baldwin R.L. Three-state analysis of sperm whale apomyoglobin unfolding. Biochemistry 1993, 32:3790-3796.
44. Beckingham J.A., Bottomley S.P., Hinton R., Sutton B.J., Gore M.G. Interactions between a single immunoglobulin-binding domain of protein L from Peptostreptococcus magnus and a human k light chain. Biochemical Journal 1999, 340:193-199.
45. Beratan D.N., Betts J.N., Onuchic J.N. Protein electron transfer rates set by the bridging secondary and tertiary structure. Science 1991, 252:1285-1288.
46. Bilsel O., Yang L., Zitzewitz J.A., Beechem J.M., Matthews C.R. Time-Resolved Fluorescence Anisotropy Study of the Refolding Reaction of the α-Subunit of Tryptophan Synthase Reveals Nonmonotonic Behavior of the Rotational Correlation Time. Biochemistry 1999, 38:4177-4187.
47. Bismuto E., Irace G., D'Auria S., Rossi M., Nucci R. Multitryptophan fluorescence-emission decay of beta-glycosidase from the extremely thermophilic archaeon Sulfolobus solfataricus. European Journal of Biochemistry 1997, 244:53-58.
48. Blat Y., Eisenbach M. Oligomerization of the phosphatase CheZ upon interaction with the phosphorylated form of CheY. The signal protein of bacterial chemotaxis. J. Biol. Chem. 1996, 271:1226-1231.
49. Bouché M.B. Lombriciens de France, écologie et systématique. Annales Zoologie et Ecologie Animale 1972, 72:1-671. (Numéro spécial).
50. Bourne Y., Van Tilbeurgh H., Cambillau C. Protein-carbohydrate interactions. Current Opinion of Structural Biology 1993, 3:681-686.
51. Brinkman-van der Linden EC, van Ommen EC, van Dijk W Glycosylation of alpha 1-acid glycoprotein in septic shock: changes in degree of branching and in expression of sialyl Lewis(x) groups. Glycoconjugate Journal 1996, 13:27-31.
52. Britz-McKibbin P., Markuszewski M.J., Iyanagi T., Matsuda K., Nishioka T., Terabe S. Picomolar analysis of flavins in biological samples by dynamic pH junction-sweeping capillary electrophoresis with laser-induced fluorescence detection. Analytical Biochemistry 2003, 313:89-96.
53. Bundy J.G., Spurgeon D.J., Svendsen C., Hankard P.K., Osborn D., Lindon J.C., Nicholson J.K. Earthworm species of the genus Eisenia can be phenotypically differentiated by metabolic profiling. FEBS letters 2002, 521:115-120.
54. Burstein E.A., Vedenkina N.S., Ivkova M.N. Fluorescence and the location of tryptophan residues in protein molecules. Photochemistry and Photobiology 1973, 18:263-279.
55. Burstein E.A., Emelyanenko V.L. Log-normal description of fluorescence spectra of organic fluorophores. Photochemistry and Photobiology 1996, 64:316-320.
56. 1-acid glycoprotein and progesterone. Journal of Biological Chemistry 1968, 243:6130-6139.
57. Cantor C.R., Schimmel P.R. Biophysical Chemistry 1980, Editions W. H. Freeman and Company, New York.
58. 2 and oxidized cytochrome c. Evidence for the existence of a protein complex in the reaction. European Journal of Biochemistry 1982, 128:533-542.
59. 2, an electron carrier between fiavocytochrome b, and cytochrome c: Rapid kinetic characterisation of the electron transfer parameters with ionic strength dependence. Biochemical Journal 1987, 245:159-165.
60. Carpita N.C., Gibeaut D.M. Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant Journal 1993, 3:1-30.
61. Carrero J., Jameson D.M., Gratton G. Oxygen distribution and diffusion into myoglobin revealed by quenching of zincprotoporphyrin IX fluorescence. Biophysical Chemistry 1995, 54:143-154.
62. Carter C.W., Kraut J., Freer S.T., Nguyen H.-X., Alden R.A., Bartsch R.G. Two-Angstrom crystal structure of oxidized Chromatium high potential iron protein. Journal of Biological Chemistry 1974, 249:4212-4225.
63. Casimiro D.R., Wong L.L., Colon J.L., Zewert T.E., Richards J.H., Chang I-J., Winkler J.R., Gray H.B. Electron transfer in ruthenium/zinc porphyrin derivatives of recombinant human myoglobins. Analysis of tunneling pathways in myoglobin and cytochrome c. Journal of American Chemical Society 1993, 115:1485-1489.
64. Chang Y-C., Ludescher R.D. Local conformation of rabbit skeletal myosin rod filaments probed by intrinsic tryptophan fluorescence. Biochemistry 1994, 33:2313-2321.
65. i) and the concentration of inhibitor which causes 50 per cent inhibition (150) of an enzymatic reaction. Biochemical Pharmacology 1973, 22:3099-3108.
66. Chiu K.M., Mortensen R.F., Osmand A.P., Gewurz H. Interactions of alphal-acid glycoprotein with the immune system. I. Purification and effects upon lymphocyte responsiveness. Immunology 1977, 32:997-1005.
67. Christie J.M., Salomon M., Nozue K., Wada M., Briggs W.R. LOV (light, oxygen or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide. Proc. Natl. Acad. Scien. U.S.A. 1999, 96:8779-8783.
68. Cinelli R.A.G., Ferrari A., Pellegrini V., Tyagi M., Giacca M., Beltram F. The enhanced green fluorescent protein as a tool for the analysis of protein dynamics and localization: Local fluorescence study at the single-molecule level. Photochemistry and Photobiology 2004, 71:771-776.
69. Clayton A.H.A., Sawyer W.H. Tryptophan rotamer distributions in amphipathic peptides at a lipid surface. Biophysical Journal 1999, 76:3235-3242.
70. Collins J.H., Cox J.A., Theibert J.L. Amino acid sequence of a sarcoplasmic calcium-binding protein from the sandworm Nereis diversicolor. Journal of Biological Chemistry 1988, 263:15378-15385.
71. 2. Biochemistry 1996, 35:6351-6357.
72. Dahms T.E.S., Willis K.J., Szabo A.G. Conformational heterogeneity of tryptophan in a protein crystal. Journal of The American Chemical Society 1995, 117:2321-2326.
73. Das T.K., Mazumdar S. pH-induced conformational perturbation in horseradish peroxidase. Picosecond tryptophan fluorescence studies on native and cyanide-modified enzymes. Eur. J. Biochem. 1995, 227:823-828.
74. Das T.K., Mazumdar S. Conformational substates of apoprotein of Horsedadish peroxidase in aqueous solution-a fluorescence dynamics study. J. Phys. Chem. 1995, 99:13283-13290.
75. Davis T.N., Urdea M.S., Masiarz F.R., Thorner J. Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 1986, 47:423-431.
76. De S., Girigoswami A. Fluorescence resonance energy transfer-a spectroscopic probe for organized surfactant media. Journal of Colloidal Interface Science 2004, 271:485-495.
77. De Beuckeleer K., Volckaert G., Engelborghs Y. Time resolved fluorescence and phosphorescence properties of the individual tryptophan residues of barnase: Evidence for protein-protein interactions. Proteins: Structure, Function and Genetics 1999, 36:42-53.
78. 1-acid glycoprotein (orosomucoid) and progesterone. A fluorescence study. Carbohydrate Research 2002, 337:1405-1410.
79. Demchenko A.P. Fluorescence molecular relaxation studies of protein dynamics. FEBS Letters 1985, 182:99-102.
80. Demchenko A.P. The red-edge effects: 30 years of exploration. Luminescence 2002, 17:19-42.
81. Dente L, Pizza MG, Metspalu A, Cortese R Structure and expression of the genes coding for human alpha 1-acid glycoprotein. EMBO J 1987, 6:2289-2296.
82. Devaraj S., Xu D.Y., Jialal I C-reactive protein increases plasminogen activator inhibitor-1 expression and activity in human aortic endothelial cells: implications for the metabolic syndrome and atherothrombosis. Circulation 2003, 107:398-404.
83. Dickerson R.E., Geis I Hemoglobin: structure, function, evolution and pathology 1983, The Benjamin/Cummings Publishing Company, Inc.
84. Di Venere A., Mei G., Gilardi G., Rosato N., De Matteis F., McKay R., Gratton E., Finazzi Agro A. Resolution of the heterogeneous fluorescence in multitryptophan proteins: ascorbate oxidase. European Journal of Biochemistry 1998, 257:337-343.
85. Donovan J.W. Changes in Ultraviolet Absorption Produced by Alteration of Protein Conformation. Journal of Biological Chemistry 1969, 244:1961-1967.
86. Drew J., Thistletwhaite P., Woolfe G Excited-state relaxation in 1-amino-8-naphtthalene-sulfonate. Chemical Physical Letters 1983, 96:296-301.
87. Du H., Fuh R.A., Li J., Corkan A., Lindsey J.S. PhotochemCAD: A computer-aided design and research tool in photochemistry. Photochemistry and Photobiology 1998, 68:141-142.
88. Easter J.H., DeToma R.P., Brand L. Nanosecond time-resolved emission spectroscopy of a fluorescence probe adsorbed to L-alpha-egg lecithin vesicles. Biophysical Journal 1976, 16:571-583.
89. Ebu Isaac V., Patel L., Curran T., Abate-Shen C Use of fluorescence energy transfer to estimate intramolecular distances in the Msx-1 homeodomain. Biochemistry 1995, 34:15276-15281.
90. Edwards C.A., Bohlen P.J. Biology and ecology of earthworms 1996, Chapman and Hall, London. third ed.
91. Eftink M Quenching-resolved emission anisotropy studies with single and multitryptophan-containing proteins. Biophysical Journal 1983, 43:323-334.
92. Eftink M.R., Ghiron C.A. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry 1976, 15:672-680.
93. Engelstad F., Stenersen J Acetylesterase pattern in the earthworm genus Eisenia (Oligochaeta, Lumbricidae): implications for laboratory use and taxonomic status. Soil Biology and Biochemistry 1991, 23:243-247.
94. Falk J.E. Porphyrins and metalloporphyrins 1975, Elsevier Scientific Publishing Company. S. Kevin M. (Ed.).
95. Feitelson J., Spiro T.G. Bonding in zinc proto- and mesoporphyrin substituted myoglobin and model compounds studied by resonance raman spectroscopy. Inorganic Chemistry 1986, 25:861-865.
96. Fisher C.A., Narayanaswami V., Ryan R.O. Journal of Biological Chemistry 2000, 275:33601-33606.
97. Flower D.R. Multiple molecular recognition properties of the lipocalin protein family. Journal of Molecular Recognition 1995, 8:185-195.
98. Flower D.R. The lipocalin protein family: structure and function. Biochemical Journal 1996, 318:1-14.
99. Foriers A., Wunilmart C., Sharon C., Strosberg A.D. Extensive sequence homologies among lectins from leguminous plants. Biochemical Biophysical Research Communication 1977, 75:980-986.
100. Forster T. Intermolecular energy migration and fluorescence. Annual of Physics (Leipzig) 1948, 2:55-75.
101. Frank I.M., Vavilov S.I. Über die Wirkungssphäre der Auslöschungsvargänge in den flureszierenden flüssigkeiten. Z. Phys. 1931, 69:100-110.
102. Franzen L.E., Svensson S., Larm O Structural studies on the carbohydrate portion of human antithrombin III. Journal of Biological Chemistry 1980, 255:5090-5093.
103. Frauenfelder H., Petsko C.A., Tsernoglou D. Temperature-dependent X-ray diffraction of a probe of protein structural dynamics. Nature 1979, 280:558-563.
104. Froschle M., Ulmer W., Jany K.D. Tyrosine modification of glucose dehydrogenase from bacillus megaterium. Effect of tetranitromethane on the enzyme in the tetrameric and monomeric state. European Journal of Biochemistry 1984, 142:533-540.
105. Fujimoto K., Shimizu H., Inouye M. Unambiguous Detection of Target DNAs by Excimer-Monomer Switching Molecular Beacons. Journal of Organic Chemistry 2004, 69:3271-3275.
106. Fussle R., Bhakdi S., Sziegoleit A., Tranum-Jensen J., Kranz T., Wellensiek H.J. On the mechanism of membrane damage by Staphylococcus aureus α-toxin. Journal of Cell Biology 1981, 91:83-94.
107. Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L. Crystal structure of horseradish peroxidase C at 2.15 resolution. Nature, Structural Biology 1997, 4:1032-1038.
108. Gambacorti-Passerini C, Barni R, le Coutre P, Zucchetti M, Cabrita G, Cleris L, Rossi F, Gianazza E, Brueggen J, Cozens R, Pioltelli P, Pogliani E, Corneo G, Formelli F, D'Incalci M. Role of alphal acid glycoprotein in the in vivo resistance of human BCR-ABL(+) leukemic cells to the abl inhibitor STI571. Journal of the National Cancer Institute 2000, 92:1641-1650.
109. 2-a bifunctional enzyme-into a cytochrome core and a flavoprotein molecule. Biochemical Biophysical Research Communication 1977, 77:1543-1551.
110. 2, requiring the association of two domains. European Journal of Biochemistry 1980, 111:17-31.
111. Gibney B.R., Dutton P.L. Histidine Placement in De Novo Designed Heme Proteins. Protein Science 1999, 8:1888-1898.
112. Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Analytical Biochemistry 1989, 182:283. Erratum in: Anal. Biochem., 1990.
113. Goto Y., Fink A.L. Phase diagram for acidic conformational states of apomyoglobin. Journal of Molecular Biology 1990, 214:803-805.
114. Gratton E. Frequency-domain Cross-Correlation Fluorometry with Phase-Locked Loop Frequency Synthesizers June 20, 1989, US. Patent 4,840,485.
115. Gray G.S., Kehoe M. Primary sequence of the alpha-toxin gene from Staphylococcus aureus wood. Infection and Immunity 1984, 46:615-618.
116. Grossniklaus H.E., Waring G.O., Akor C., Castellano-Sanchez A.A., Bennett K Evaluation of hematoxylin and eosin and special stains for the detection of acanthamoeba keratitis in penetrating keratoplasties. American. Journal of Ophthalmology 2003, 136:520-526. 4th.
117. Gryczynski Z., Lubkowski J., Bucci E. Heme-Protein Interactions in Horse Heart Myoglobin at Neutral pH and Exposed to Acid Investigated by Time-resolved Fluorescence in the Pico-to Nanosecond Time Range. Journal of Biological Chemistry 1995, 270:19232-19237.
118. Gryczynski Z, Bucci E. Time resolved emissions in the picosecond range of single tryptophan recombinant myoglobins reveal the presence of long range heme protein interactions. Biophysical Chemistry 1998, 74:187-196.
119. Hagihara Y., Aimoto S., Fink A.L., Goto Y. Guanidine hydrochloride-induced folding of proteins. Journal of Molecular Biology 1993, 231:180-184.
120. Harada S., Kitadokoro K., Kinoshita T., Kai Y., Kasai N. Crystallization and main-chain structure of neutral protease from Streptomyces caespitosus. Journal of Biochemistry 1991, 110:46-49.
121. Hatton M.W.C., Marz L., Berry L.R., Debanne M.T., Regoeczi E. Biand tri-antennary human transferrin glycopeptides and their affinities for the hepatic lectin specific for asialo-glycoproteins. Biochemical Journal 1979, 181:633-638.
122. Heim R., Cubitt A.B., Tsien Y. Improved green fluorescence. Nature 1995, 373:663-664.
123. Heim R Green fluorescent protein forms for energy transfer. Methods in Enzymology 1999, 302:408-423.
124. Heyduk T, Heyduk E Molecular beacons for detecting DNA binding proteins. Nature Biotechnology 2002, 20:171-176.
125. Hirsch R.E., Zukin S.R., Nagel R.L. Intrinsic fluorescence emission of intact oxy hemoglobins. Biochemical Biophysical Research Communications 1980, 93:432-439.
126. Hirsch R.E., Nagel R.L. Conformational studies of hemoglobins using intrinsic fluorescence measurements. Journal of Biological Chemistry 1981, 256:1080-1083.
127. Hirshfield K.M., Toptygin D., Grandhige G., Kim H., Packard B.Z., Brand L Steady-state and time-resolved fluorescence measurements for studying molecular interactions: interaction of a calcium-binding probe with proteins. Biophysical Chemistry 1996, 62:25-38.
128. Hof M., Vajda S., Fidler V, Karpenko V Picosecond tryptophan fluorescence of human blood serum orosomucoid. Collect. Czech. Chem. Commun. 1996, 61:808-818.
129. 1H NMR study. Biophysical Chemistry 1996, 61:151-160.
130. Hyde C.C., Ahmed S.A., Padlan E.A., Miles E.W., Davies D.R. Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. Journal of Biological Chemistry 1988, 263:17857-17871.
131. Ichikawa T., Terada H. Second derivative spectrophotometry as an effective tool for examining phenylalanine residues in proteins. Biochimica Biophysica Acta 1977, 494:267-270.
132. Ichikawa T., Terada H. Estimation of state and amount of phenylalanine residues in proteins by second derivative spectrophotometry. Biochimica Biophysica Acta 1979, 580:120-128.
133. Itoh M., Mizukoshi H., Fuke K., Matsukawa S., Mawatari K., Yoneyama Y., Sumitani M., Yoshihara Y. Tryptophan fluorescence of human hemoglobin. I. Significant change of fluorescence intensity and lifetimes in the T-R transition. Biochemical Biophysical Research Communications 1981, 100:1259-1265.
134. Jablonski A. Über den Mechanismus des Photolumineszens von Farbstoffphosphoren. Z. Phys. 1935, 94:38-64.
135. Jaenike J. "Eisenia foetida" is two biological species. Megadrilogica 1982, 4:6-7.
136. James D.R., Siemiarczuk A., Ware W.R. Stroboscopic optical boxcar technique for the determination of fluorescence lifetimes. Review of Scientific Instrument. 1992, 63:1710-1716.
137. desFe. Multifrequency phase and modulation fluorometry study. Biophysical Journal 1984, 45:795-803.
138. 1-acid glycoprotein expressed in the plasma of chronic myeloid leukemia patients does not mediate significant in vitro resistance to STI571. Blood 2002, 99:713-715.
139. Jullien M., Garel J-R., Merola F., Brochon J-C Quenching by acrylamide and temperature of a fluorescent probe attached to the active site of ribonuclease. European Biophysical Journal 1986, 13:131-137.
140. Kabsch W., Mannherrz H.G., Shuck D., Pai E.F., K.C.Holmes Atomic structure of actin: DNase I complex. Nature 1990, 347:37-44.
141. Karplus M., McCammon J.A. Dynamics of proteins: Elements and function. Annual Review of Biochemistry 1983, 53:263-300.
142. Kauzmann W. Quantum Chemistry 1957, Academic Press.
143. Kehoe M., Duncan I., Foster T., Fairweather N., Dougan G Cloning, expression, and mapping of the Staphylococcus aureus alpha-hemolysin determinant in Escherichia coli K-12. Infection and Immunity 1983, 4:1105-1111.
144. Khan K.K., Mazumdar S., Modi S., Sutcliffe M., Roberts G.C.K., Mitra S. Steady-state and picosecond-time-resolved fluorescence studies on the recombinant heme domain of Bacillus megaterium cytochrome P-450. European Journal of Biochemistry 1997, 244:361-370.
145. Khan M.J., Joginadha Swamy M., Krishna Sastry M.V., Umadevi Sajjan S., Patanjali S.R., Rao P., Swarnalatha G.V., Banerjee P., Surolia A. Saccharide binding to three Gal/GalNac specific lectins: Fluorescence, spectroscopic and stopped-flow kinetic studies. Glycoconjugate Journal 1988, 5:75-84.
146. Kirby E.P., Steiner R.F. The tryptophan microenvironments in apomyoglobin. Journal of Biological Chemistry 1970, 245:6300-6630.
147. Kirley T.L., Spargue E.D., Halsall H.B. The binding of spin-labeled propranolol and spin labeled progesterone by orosomucoid. Biophysical Chemistry 1982, 15:209-216.
148. Kiss R.S., Kay C.M., Ryan R.O. Amphipathic α-helix bundle organization of lipid-free chicken apolipoprotein A-I. Biochemistry 1999, 38:4327-4334.
149. Kita A., Kasai N., Kasai S., Nakaya T., Miki K. Crystallization and preliminary X-ray diffraction studies of a flavoprotein, FP390, from a luminescent bacterium, Photobacterium phosphoreum. Journal of Biochemistry 1991, 110:748-750.
150. 1-acid glycoprotein and its high-affinity binding site. Biochemical Biophysical Research Communications 2003, 300:41-46.
151. Kornfeld K., Reitman M-L, Kornfeld R The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant. Journal of Biological Chemistry 1981, 256:6633-6640.
152. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. Journal of Applied Crystallography 1991, 24:946-950.
153. Krishna M.M., Periasamy N. Spectrally constrained global analysis of fluorescence decays in biomembrane systems. Analytical Biochemistry 1997, 253:1-7.
154. Kubota Y., Matado Y., Shi-Genuare Y., Fujisaki Y. Fluorescence quenching of 10-methylacridinium chloride by nucleotides. Photochemistry and Photobiology 1979, 29:1099-1106.
155. Kuipers O.P., Vincent M., Brochon J-C, Verheij H.M., De Haas G.H., Gallay J. Insight into the conformational dynamics of specific regions of porcine pancreatic phospholipase A2 from a time-resolved fluorescence study of a genetically inserted single tryptophan residue. Biochemistry 1991, 30:8771-8785.
156. kungl A.J., Visser N.V., van Hoek A., Visser A.J., Billich A., Schilk A., Gstach H., Auer M. Time-resolved fluorescence anisotropy of HIV-1 protease inhibitor complexes correlates with inhibitory activity. Biochemistry 1998, 37:2778-2786.
157. Kunz L., MacRobert A.J. Intracellular photobleaching of 5,10,15,20-tetrakis(m-hydroxyphenyl) chlorin (Foscan) exhibits a complex dependence on oxygen level and fluence rate. Photochemistry and Photobiology 2002, 75:28-35.
158. Kuppens S., Hellings M, Jordens J, Verheyden S, Engelborghs Y Conformational states of the switch I region of Ha-ras-p21 in hinge residue mutants studied by fluorescence lifetime and fluorescence anisotropy measurements. Protein Science 2003, 12:930-938.
159. Kute T, Westphal U Steroid-protein interactions. XXXIV. Chemical modification of alphal-acid glycoprotein for characterization of the progesterone binding site. Biochimica Biophysica Acta 1976, 420:195-213.
160. 2 (L-lactate: cytochrome c oxidoreductase). European Journal of Biochemistry 1972, 25:33-40.
161. Ladokhin A.S., White S.H. Alphas and Taus of Tryptophan Fluorescence in Membranes. Biophysical Journal 2001, 181:1825-1827.
162. Lahiri B., Bagdasarian A., Mitchell B., Talamo R.C., Colman R.W., Rosenberg R.D. Antithrombin-Heparin Cofactor: An inhibitor of plasma kallikrein. Archives of Biochemistry and Biophysics 1976, 175:737-747.
163. Lakowicz J.R., Weber G. Quenching of fluorescence by oxygen. A probe for structural fluctuation in macromolecules. Biochemistry 1973, 12:4161-4170.
164. Lakowicz, Maliwal Oxygen quenching and fluorescence depolarization of tyrosine residues in proteins. Journal of Biological Chemistry 1983, 258:4794-4801.
165. Lakowicz J.R., Maliwal B., Cherek H., Balter A. Rotational freedom of tryptophan residues in proteins and peptides. Biochemistry 1983, 22:1741-1752.
166. Lakowicz J.R., Gratton E., Cherek H., Maliwal B.P., Laczko G. Determination of time-resolved fluorescence emission spectra and anisotropies at a fluorophore-protein complex using frequency-domain phase-modulation fluorometry. Journal of Biological Chemistry 1984, 259:10967-10972.
167. Lakowicz J.R., Laczko G., Gryczinski I. 2-GHz frequency-domain fluorometer. Review of Scientific Instrumunents 1985, 57:2499-2506.
168. Lakowicz J.R. Principles of Fluorescence Spectroscopy 1999, Kluwer Academic/Plenum Publishers, New York.
169. Lawson D.M., Derewenda U., Serre L., Ferri S., Szittner R., Wei Y., Meighen E.A., Derewenda Z.S. Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi. Biochemistry 1994, 33:9382-9388.
170. Lee J-S., Liao J-H., Wu S-H., Chiou S.H. α-Crystallin acting as a molecular chaperonin against photodamage by UV irradiation. Journal of Protein Chemistry 1997, 16:283-289.
171. Lee S.Y. NMR Studies of calmodulin from S. cerevisiae. Ph. D. thesis. 2000, University of Washington.
172. Lee S.Y., Klevit R.E. The whole is not the simple sum of its parts in calmodulin from S. cerevisiae. Biochemistry 2000, 39:4225-4230.
173. Leenders R., Van Hoek A., Van lersel M., Veeger C., Visser A.J.W.G. Flavin dynamics in oxidized C/ostridium beijerinckii flavodoxin as assessed by timeresolved polarized fluorescence. European Journal of Biochemistry 1993, 218:977-984.
174. Lehrer S.S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 1971, 10:3254-3263.
175. Le Tilly V., Royer C. Fluorescence anisotropy assays implicate proteinprotein interactions in regulating trp repressor DNA binding. Biochemistry 1993, 32:7753-7758.
176. Li J., Szittner R., Meighen E.A. Tryptophan Fluorescence of the lux-Specific Vibrio harveyi Acyl-ACP Thioesterase and Its Tryptophan Mutants: Structural Properties and Ligand-Induced Conformational Change. Biochemistry 1998, 37:16130-16138.
177. 5: effect of methylating the heme propionates of zn-myoglobin. Journal of The American Chemical Society 2000, 122:3552-3553.
178. 5. Journal of The American Chemical Society 2002, 124:6849-6859.
179. Libich D.S., Hill C.M., Bates I.R., Hallett F.R., Armstrong S., Siemiarczuk A, Harauz G Interaction of the 18.5-kD isoform of myelin basic protein with Ca2+-calmodulin: effects of deimination assessed by intrinsic Trp fluorescence spectroscopy, dynamic light scattering, and circular dichroism. Protein Science 2003, 12:1507-1521.
180. Liener I.E. Phytohemagglutinins (Phytolectins). Annual Review of Plant Physiology 1976, 27:291-319.
181. Lin J.K. Mechanisms of cancer chemoprevention by curcumin. Proc. Natl. Sci. Commun., BOC(B) 2001, 25:59-66.
182. Livesey A.K., Brochon J-C. Analyzing the distribution of decay constants in pulse-fluorimetry using the maximum entropy method. Biophysical Journal 1987, 52:693-706.
183. Loebel D., Scaloni A., Paolini S., Fini C., Ferrara L., Breer H., Pelosi P. Cloning, post-translational modifications, heterologous expression and ligand-binding of boar salivary lipocalin. Biochemical Journal 2000, 350(Part 2):369-379.
184. Lopez Ý Arbeloa F., Ruiz Ý Ojeda P., Lopez Ý Arbeloa I. Fluorescence self-quenching of the molecular forms of rhodamine B in aqueous and ethanolic solutions. Journal of Luminescence 1989, 44:105-112.
185. Loris R., Steyaert J., Maes D., Lisgarten J., Pickersgill R., Wyns L. Crystal structure determination and refinement at 2.3- resolution of the lentil lectin. Biochemistry 1993, 32:8772-8781.
186. Loskutoff D.J., Schleef R.R. Plasminogen activators and their inhibitors. Methods in Enzymology 1988, 163:293-302.
187. Maeda H, Ishida N Specificity of binding of hexopyranosyl polysaccharides with fluorescent brightener. Journal of Biochemistry 1967, 62:276-278.
188. Margalit R., Shaklai N., Cohen S Fluorometric studies on the dimerization equilibrium of protoporphyrin IX and its haemato derivative. Biochemical Journal 1983, 209:547-552.
189. MacPhee C.A., Howlett G.J., Sawyer W.H., Clayton A.H.A. Helix-Helix Association of a Lipid-Bound Amphipathic α-Helix Derived from Apolipoprotein C-II. Biochemistry 1999, 38:10878-10884.
190. 1-acid glycoprotein as markers of inflammation and cancer. Glycoconjugate Journal 1995, 12:241-247.
191. Majoul I., Straub M., Duden R., Hell S.W., Soling H.D. Fluorescence resonance energy transfer analysis of protein-protein interactions in single living cells by multifocal multiphoton microscopy. Journal of Biotechnology 2002, 82:267-277.
192. Malicka J., Gryczynski I., Fang J., Kusba J., Lakowicz J.R. Increased resonance energy transfer between fluorophores bound to DNA in proximity to metallic silver particles. Analitical Biochemistry 2003, 315:160-169.
193. Maliwal B.P., Kusba J., Lakowicz J.R. Fluorescence energy transfer in one dimension: Frequency-domain fluorescence study of DNA-fluorophore complex. Biopolymers 1995, 35:245-255.
194. 1 antitrypsin and antithrombin-III. The Physiological Inhibitions of Blood Coagulation and Fibrinolysis 1979, 43. Elsevier/North-Holland Biomedical Press, Amsterdam, The Netherlands. D.W. Collen, B. Wiman, M. Verstraete (Eds.).
195. Marcus R.A., Sutin N. Electron Transfers in Chemistry and Biology. Biochimica Biophysica Acta 1985, 811:265-322.
196. Matthews B.W. Solvent content of protein crystals. Journal of Molecular Biology 1968, 33:491-497.
197. Matthews C.R., Crisanti M.M. Urea-induced unfolding of the α-subunit of tryptophan synthase: evidence for a multistate process. Biochemistry 1981, 20:784-792.
198. Matulis D, Lovrien R. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophysical Journal 1998, 74:422-429.
199. Matulis D., Baurmann C.G., Bloomfield V.A., Lovrien R.E. 1-anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopolymers 1999, 49:451-458.
200. Marz L., Hatton M.W., Berry L.R., Regoeczi E The structural heterogeneity of the carbohydrate moiety of desialylated human transferrin. Canadian Journal of Biochemistry 1982, 60:624-630.
201. McClure W.O., Edelman G.M. Fluorescent probes for conformational states of proteins. 1. Mechanism of fluorescence of 2-p-toluidinylnaphthalene. 6-sulfonate. A hydrophobie probe. Biochemistry 1966, 5:1908-1918.
202. McPherson A., Mickelson K.E., Westphal U. Crystallization of corticosteroid binding globulin (CBG) and alpha 1-acid glycoprotein (AAG). Journal of Steroid Biochemistry 1980, 13:991-992.
203. 1-acid lipoprotein. Biochemical Biophysical Research Communications 1984, 124:619-624.
204. Meagher J.L., Beechem J.M., Olson S.T., Gettins P.G.W. Deconvolution of the fluorescence emission spectrum of human antithrombin and identification of the tryptophan residues that are responsive to heparin binding. Journal of Biological Chemistry 1998, 273:23283-23289.
205. Megan L.J., Kurnikov I.V., Beratan D.N. The nature of tunneling pathway and average packing density models for protein-mediated electron transfer. Journal of Physical Chemistry A. 2002, 106:2002-2006.
206. Mehta K., Pantazis P., McQueen T., Agarwal B. Antiproliferative effect of curcumin against human breast tumor cell lines. Anticancer Drugs. 1997, 8:471-480.
207. Mei G., Di Venere A., Campeggi F.M., Gilardi G., Rosato N., De Matteis F., Finazzi-Agrò A. The effect of pressure and guanidine hydrochloride on azurins mutated in the hydrophobic core. European Journal of Biochemistry 1999, 265:619-626.
208. Menache D. Antithrombin III: Introduction. Semin Hematol 1991, 28:1-2.
209. Menache D., Grossman B., Jackson C Antithrombin III: Physiology, deficiency, and replacement therapy. Transfusion 1992, 32:580-588.
210. Menestrina G. Ionic channel formed by Staphylococcus aureus α-toxin: voltage-dependent inhibition by divalent and trivalent cations. Journal of Membrane Biology 1986, 90:177-190.
211. Messerschmidt A., Rossi A., Landenstein R., Huber R., Bolognesi M., Gatti G., Marchesini A., Petruzzelli R., Finazzi Agro A. X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Journal of Molecular Biology 1989, 206:513-529.
212. Messerschmidt A., Landenstein R., Huber R., Bolognesi M., Avigliano L., Petruzzelli R., Rossi A., Finazzi Agro A. Refined crystal structure of ascorbate oxidase at 1.9 resolution. Journal of Molecular Biology 1992, 224:179-205.
213. Miki K., Ezoe T., Masui A., Yoshisaka T., Mimuro M., Fujiwara-Arasaki T., Kasai N. Crystallization and preliminary X-ray diffraction studies of C-phycocyanin from a red alga, Porphyra tenera. Journal of Biochemistry 1990, 108:646-649.
214. Molecular Probes Handbook of fluorescent probes and research chemicals 1992-1994.
215. Monsigny M., Roche A.C., Sene C., Maget-Dana R., Delmotte F Sugarlectin interactions: How does wheat-germ agglutinin bind sialoglycoconjugates?. European Journal of Biochemistry 1980, 104:147-153.
216. The Annexins 1992, Portland Press, Ltd, London. S.E. Moss (Ed.).
217. Nagatomo S., Nagai M., Shibayama N., Kitagawa T Differences in changes of the alphal-beta2 subunit contacts between ligand binding to the alpha and beta subunits of hemoglobin A: UV resonance raman analysis using Ni-Fe hybrid hemoglobin. Biochemistry 2002, 41:10010-10020.
218. c-21 and inhibition of substrate binding by acrylamide. Biochemistry 1988, 27:1147-1153.
219. suc1 from Schizosaccharomyces pombe. Journal of Biological Chemistry 1996, 271:27249-27258.
220. Nishimura C., Riley R., Eastman P., Fink A.L Fluorescence energy transfer indicates similar transient and equilibrium intermediates in staphylococcal nuclease folding. Journal of Molecular Biology 2000, 299:1133-1146.
221. Ntziachristos N., Chance B. Breast imaging technology: Probing physiology and molecular function using optical imaging-applications to breast cancer. Breast Cancer Research 2001, 3:41-46.
222. 2+ exchange on the flexibility and/or conformation of the small domain in monomeric actin. Biophysical Journal 1998, 74:2474-2481.
223. O'Connell M.A., Gerber A., Keller W. Purification of human double-stranded RNA-specific editase 1 (hRED1) involved in editing of brain glutamate receptor B pre-mRNA. Journal of Biological Chemistry 1997, 272:473-478.
224. OECD Draft Document OECD guideline for the testing of chemicals. Earthworm reproduction test (Eisenia fetida/andrei) January 2000.
225. Ogul'chansky T.Y., Losytskyy M.Yu, Kovalska V.B., Yashchuk V.M., Yarmoluk S.M. Interactions of cyanine dyes with nucleic acids. XXIV. Aggregation of monomethine cyanine dyes in presence of DNA and its manifestation in absorption and fluorescence spectra. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2001, 57:1525-1532.
226. 2+ on target recognition by calmodulin. Biochemistry 1997, 36:4309-4316.
227. Oien N., Stenersen J Esterases of earthworms-III. Electrophoresis reveals that Eisenia fetida (Savigny) is two species. Comparative Biochemistry and Physiology 1984, 78C:277-282.
228. Oton J, Franchi D, Steiner R.F., Martinez C.F., Bucci E. Fluorescence studies of internal rotation in apohemoglobin alpha-chains. Archives of Biochemistry and Biophysics 1984, 228:519-524.
229. Page C.C., Moser C.C., Chen X., Dutton P.L Natural engineering principles of electron tunneling in biological oxidation-reduction. Nature 1999, 402:47-52.
230. Parisini E., Capozzi F., Lubini P., Lamzin V., Luchinat C., Sheldrick G.M. Ab initio solution and refinement of two high potential iron protein structures at atomic resolution. Acta Crystallography D. 1999, 55:1773-1784.
231. Parikh H.H., McElwain K., Balasubramanian V., Leung W., Wong D., Morris M.E., Ramanathan M. A rapid spectrofluorimetric technique for determining drug-serum protein binding suitable for high-throughput screening. Pharmaceutical Research 2000, 17:632-637.
232. Perotti C., Fukuda H., DiVenosa G., MacRobert A.J., Batlle A., Casas A. Porphyrin synthesis from ALA derivatives for photodynamic therapy. In vitro and in vivo studies. British Journal of Cancer. 2004, 90:1660-1665.
233. Perutz M.F. Stereochemistry of cooperative effects in haemoglobin. Nature 1970, 228:726-739.
234. Pervais S., Brew K. Homology of beta-lactoglobulin, serum retinol-binding protein and protein HC. Science 1985, 228:335-337.
235. Piston D.W., Masters B.R., Webb W.W. Three-dimensionally resolved NAD(P)H cellular metabolic redox imaging of the in situ cornea with two-photon excitation laser scanning microscopy. Journal of Microscopy 1995, 178:20-27.
236. Privat J.P., Wahl P., Auchet J.C. Rates of deactivation processes of indole derivatives in water-organic solvent mixtures--application to tryptophyl fluorescence of proteins. Biophysical Chemistry 1979, 9:223-233.
237. Pjura P.E., Grzeskowiak K, Dickerson R.E. Binding of Hoechst 33258 to the minor groove of B-DNA. Journal of Molecular Biology 1987, 197:257-271.
238. Poveda J.A., Prieto M., Encinar J.A., González-Ros J.M., Mateo C.R. Intrinsic Tyrosine Fluorescence as a Tool To Study the Interaction of the Shaker B "Ball" Peptide with Anionic Membranes. Biochemistry 2003, 42:7124-7132.
239. Prats M Complexes between L (+) lactate: cytochrome c oxidoreductases from the yeasts Saccharomyces cerevisiae or Hansenula anomala and horse heart cytochrome c. Biochimie 1977, 59:621-626.
240. Rachofsky E.L., Osman R., Ross J.B. Probing structure and dynamics of DNA with 2-aminopurine: effects of local environment on fluorescence. Biochemistry 2001, 40:946-956.
241. Ragone R., Colonna G., Balestrieri C., Servillo L., Irace G. Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry 1984, 23:1871-1875.
242. Raja S.M., Rawat S.S., Chattopadhyay A., Lala A.K. Localization and Environment of Tryptophans in Soluble and Membrane-Bound States of a Pore-Forming Toxin from Staphylococcus aureus. Biophysical Journal 1999, 76:1469-1479.
243. Rattee I.D., Greur M.M. The Physical Chemistry of Dye absorption 1974, Academic Press, New York.
244. Rao Ch.M., Rao S.C., Rao P.B. Red edge excitation effect in intact eye lens. Photochemistry and photobiology 1989, 50:399-402.
245. Ramasamy S.M., Senthilnathan V.P., Hurtubise R.J. Determination of room-temperature fluorescence and phosphorescence quantum yields for compounds adsorbed on solid surfaces. Analytical Chemistry 1986, 58:612-616. 1986.
246. Ray S., Mukherji S., Bhaduri A. Two tryptophans at the active site of UDP-glucose 4-epimerase from Kluyveromyces fragilis. J. Biol. Chem. 1995, 270:11383-11390.
247. Renoir J.-M., Mercier-Bodard C., Hoffmann K., LeBihan S., Ning Y.-M., Sanchez E.R., Handschumacher R.E., Baulieu E.-E. Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyltransferase activity in LMCAT cells: a possible role for different heat shock protein-binding immunophilins in glucocorticosteroid receptor-mediated gene expression. Proceedings of Natural Academy of Sciences. U.S.A. 1995, 92:4977-4981.
248. Rholam M., Scarlata S., Weber G. Frictional resistance to the local rotations of fluorophores in proteins. Biochemistry 1984, 23:6793-6796.
249. Riccio A., Vitagliano L., di Prisco G., Zagari A., Mazzarella L The crystal structure of a tetrameric hemoglobin in a partial hemichrome state. Proceedings of Natural Academy of Sciences. U.S.A. 2002, 99:9801-9806.
250. Riordan J.F., Wacker W.E.C., Vallee B.L. Tetranitromethane. A reagent for the nitration of tyrosine and tyrosyl residues of proteins. Journal of The American Chemical Society 1966, 88:4104-4105.
251. Roch P., Valembois P., Lassegues M. Biochemical particulars of the antibacterial factor of the two subspecies Eisenia fetida fetida and Eisenia fetida andrei. American Society of Zoologists 1980, 20:794.
252. Rosenberg R.D., Bauer K.A., Marcum J.A. Antithrombin III, the heparin antithrombin system. Reviews in Hematology 1986, 2:351-416.
253. Rouvière N., Vincent M., Craescu C., Gallay J Immunosuppressor binding to the immunophilin FKBP59 affects the local structural dynamics of a surface beta-strand: time-resolved fluorescence study. Biochemistry 1997, 36:7339-7352.
254. Royer C.A., Tauc P., Hervé G., Brochon J-C Ligand binding and protein dynamics: a fluorescence depolarization study of aspartate transcarbamylase from Escherichia coli. Biochemistry 1987, 26:6472-6478.
255. Ruan K.-C., Weber G Physical heterogeneity of muscle glycogen phosphorylase revealed by hydrostatic pressure dissociation. Biochemistry 1993, 32:6295-6301.
256. Ruan K, Balny C High pressure static fluorescence to study macromolecular structure-function. Biochimica Biophysica Acta. Proteins and Proteomics 2002, 1595:94-102.
257. Rye H.S., Yue S., Wemmer D.E., Quesada M.A., Haugland R.P., Mathies R.A., Glazer A.N. Stable fluorescent complexes of double-stranded DNA with bis- intercalating asymmetric cyanine dyes: properties and applications. Nucleic Acids Research 1992, 20:2803-2812.
258. Safo M.K., Burnett J.C., Musayev F.N., Nokuri S., Abraham D.J. Structure of human carbonmonoxyhemoglobin at 2.16: a snapshot of the allosteric transition. Acta Crystallography D. 2002, 58:2031-2037.
259. Sagan S., Amiche S., Delfour A., Mor A., Camus A., Nicolas P. Molecular determinants of receptor affinity and selectivity of the natural delta-opioid agonist, dermenkephalin. Journal of Biological Chemistry 1989, 264:17100-17160.
260. Sager G., Nilsen O.G., Jackobsen S Variable binding of propranolol in human serum. Biochemical Pharmacology 1979, 28:905-911.
261. Sagot I., Bonneu M., Balguerie A., Aigle M. Imaging fluorescence resonance energy transfer between two green fluorescent proteins in living yeast. FEBS Letters 1999, 447:53-57.
262. Sassaroli M., Bucci E., Liesegang J., Fronticelli C., Steiner R.F. Specialized functional domains in hemoglobin: dimensions in solution of the apohemoglobin dimer labeled with fluorescein iodoacetamide. Biochemistry 1984, 23:2487-2491.
263. Sau A.K., Chen C.A., Cowan J.A., Mazumdar S., Mitra S. Steady-State and Time-Resolved Fluorescence Studies on Wild Type and Mutant Chromatium vinosum High Potential Iron Proteins: Holo- and Apo-Forms. Biophysical Journal 2001, 81:2320-2330.
264. Sato K., Nishina Y., Shiga K. Purification of Electron-Transferring Flavoprotein from Megasphaera elsdenii and Binding of Additional FAD with an Unusual Absorption Spectrum. Journal of Biochemistry 2003, 134:719-729.
265. Scarlata S., Rholam M., Weber G. Frictional resistance to local rotations in aromatic fluorophores in some small peptides. Biochemistry 1984, 23:6789-6792.
266. Schaberle F.A., Kuz'min V.A., Borissevitch I.E. Spectroscopic studies of the interaction of bichromophoric cyanine dyes with DNA. Effect of ionic strength. Biochimica Biophysica Acta 2003, 1621:183-191.
267. desFe, University of Paris 7.
268. Shaanan B., Lis H., Sharon N. Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science 1991, 254:862-866.
269. Sharma O.P. Antioxidant activity of curcumin and related substances. Biochemical Pharmacology 1976, 25:1811-1812.
270. Schmid K. Preparation and properties of serum and plasma proteins. XXIX. Separation from human plasma of polysaccharides, peptides and proteins of low molecular weight. Crystallization of an acid lipoprotein. Journal of The American. Chemical. Society 1953, 75:60-68.
271. 1-acid glycoprotein. The complete amino acid sequence, multiple amino acid substitutions, and homology with the immunoglobulins. Biochemistry 1973, 12:2711-2724.
272. Schmid F.X. Catalysis and assistance of protein folding. Curruent Opinion of Structural Biology 1991, 1:36-41.
273. Shea M.A., Verhoevenn A.S., Pedigo S Calcium-induced interactions of calmodulin domains revealed by quantitative thrombin footprinting of Arg37 and Arg106. Biochemistry 1996, 35:2943-2957.
274. Siano D.B., Metzler D.E. Band shapes of the electronic spectra of complex molecules. Journal of Chemical Physics 1969, 51:1856-1861.
275. Sillen A., Verheyden S., Delfosse L., Braem T., Robben J., Volckaert G., Engelborghs Y. Mechanism of fluorescence and conformational changes of the sarcoplasmic calcium binding protein of the sand worm Nereis diversicolor upon Ca2+ or Mg2+ binding. Biophysical Journal 2003, 85:1882-1893.
276. 1-acid glycoprotein in rheumatoid arthritis. Journal of Chromatography B Biomedical Applications 1994, 661:7-14.
277. Soengas M.S., Reyes Mateo C., Salas M., Ulises Acuña A., Gutiérrez C. Structural Features of 29 Single-stranded DNA-binding Protein. I. Environment of tyrosines in terms of complex formation with DNA. J. Biol. Chem. 1997, 272:295-302.
278. Sopkova J., Reneouard M., Lewit-Bently A. The crystal structure of a new high-calcium form of annexin V. Journal of Molecular Biology 1993, 234:816-825.
279. Sopkova J., Gallay J., Vincent M., Pancoska P., Lewit-Bentley A. The dynamic behavior of annexin V as a function of calcium ion binding: a circular dichroism, UV absorption, and steady-state and time-resolved fluorescence study. Biochemistry 1994, 33:4490-4499.
280. Spencer R.D. PHD thesis 1970, Fluorescence lifetimes: theory, instrumentation and application of nanosecond fluorometry. Published by: University Microfilms International, University of Illinois at Urbana Champaign.
281. Spinelli S., Vincent F., Pelosi P., Tegoni M., Cambillau C. Boar salivary lipocalin. Three-dimensional X-ray structure and androsterol/androstenone docking simulations. European Journal of Biochemistry 2002, 269:2449-2456.
282. Sridhar M.S., Sharma S. Microsporidial keratoconjunctivitis in a HIV-seronegative patient treated with debridement and oral itraconzaole. American Journal of Ophthalmology 2003, 136:745-746.
283. Srinivasan R., Rose G.D. The T-to-R Transformation in Hemoglobin: A Reevaluation. Proceedings of Natural Academy of Sciences USA 1994, 91:11113-11117.
284. Steiner R.F., Norris L. Fluorescence dynamics studies of troponin c. Biopolymers 1987, 26:1189-1204.
285. Stern O, Volmer M. Uber die Abklingungszeit der Fluoreszenz. Physikalische Zeitschrift 1919, 20:183-188.
286. Stolle-Smits T., Gerard Beekhuizen J., Kok M.T.C., Pijnenburg M., Jan Derksen K.R., Voragen A.G.J. Changes in Cell Wall Polysaccharides of Green Bean Pods during Development. Plant Physiology 1999, 121:363-372.
287. 1H NMR Experiments. Biochemistry 1999, 38:5065-5075.
288. Strickland S., Palmer G., Massey V. Determination of discociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data. Journal of Biological Chemistry 1975, 250:4048-4052.
289. Struck D.K., Hoekstra D., Pagano R.E. Use of resonance energy transfer to monitor membrane fusion. Biochemistry 1981, 20:4093-4099.
290. Stryer L. The interaction of a naphthalene dye with aponyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. Journal of Molecular Biology 1965, 13:482-495.
291. Szabo A.G., Krajcarski D., Zuker M., Alpert B. Conformational heterogeneity in hemoglobin as determined by picosecond fluorescence decay measurements of the tryptophan residues. Chemical Physical letters 1984, 108:145-149.
292. Swaminathan R., Nath U., Udgaonkar J.B., Periasamy N., Krishnamoorthy G. Motional Dynamics of a Buried Tryptophan Reveals the Presence of Partially Structured Forms during Denaturation of Barstar. Biochemistry 1996, 35:9150-9157.
293. Tadokoro H. Structure of Crystalline Polymers 1979, John Wiley and Sons, New York.
294. Tahirov T.H., Lu T.H., Liaw Y.C., Chen Y.L., Lin J.Y. Crystal structure of abrin-a, at 2.14. Journal of Molecular Biology 1995, 250:354-367. Erratum in: Journal of Molecular Biology 1995, 252, 154.
295. Tai P.-K.K., Albers M.W., McDonnell D.P., Chang H., Schreiber S.L., Faber L.E. Potentiation of progesterone receptor-mediated transcription by the immunosuppressant FK506. Biochemistry 1994, 33:10666-10671.
296. Talbott L.D., Ray P.M. Molecular size and separability features of pea cell wall polysaccharides: implications for models of primary structure. Plant Physiology 1992, 98:357-368.
297. Tanford C., Kawahara K., Lapanje S. Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. Journal of The American Chemical Society 1967, 89:729-736.
298. 2 and cytochrome c. Proteins: Structure, Function and Genetics 1993, 16:408-422.
299. Teilum K., Maki K., Kragelund B.B., Poulsen F.M., Roder H. Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proceedings of the Natural Academy of Sciences. U.S.A. 2002, 99:9807-9812.
300. Thomas M.A., Gervais M., Favoudon V., Valat P. Study of the Hansenula anomala yeast flavocytochrome-b2-cytochrome-c complex 2. Localization of the main association area. European Journal of Biochemistry 1983, 135:577-581.
301. Tomlin A.D., Miller J.J. Development and fecundity of the manure worm, Eisenia fetida (Annelida: Lumbricidae) under laboratory conditions. Proceedings of Seventh International Soil Zoology Colloquium, Syracuse, New York 1989, 673-678. D.L. Dindal (Ed.).
302. Travis J., Salvesen G.S. Human plasma proteinase inhibitors. Annual Review of Biochemistry 1983, 52:655-709.
303. Truong T., Bersohn R., Brumer P., Luk C.K., Tao T. Effect of pH on the phosphorescence of tryptophan, tyrosine and proteins. Journal of Biological Chemistry 1967, 242:2979-2985.
304. Truong K., Ikura M. The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Current Opinion, of Structural Biology 2001, 11:573-578.
305. Tsai C.H., Simplaceanu V., Ho N.T., Shen T.J., Wang D., Spiro, Ho C. Site mutations disrupt inter-helical H-bonds (alpha14W-alpha67T and beta15W-beta72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation. Biophysical Chemistry 2003, 100:131-142.
306. Turoverov K.K., Biktashev A.G., Khaitlina S.Y., Kuznetsova I.M. The Structure and Dynamics of Partially Folded Actin. Biochemistry 1999, 38:6261-6269.
307. 1-acid glycoprotein (orosomucoid). Biochemical. Journal 1991, 280:277-280.
308. 1-acid glycoprotein (orosomucoid): correlated thermodynamic factors and molecular parameters of polarity. Biochemical Journal 1995, 306:545-549.
309. Unzai S., Eich R., Shibayama N., Olson J., Morimoto H.J. Rate constants for O2 and CO binding to the alpha and beta subunits within the R and T states of human hemoglobin. Journal of Biological Chemistry 1998, 273:23150-23159.
310. b excitations bands. Photochem. Photobiol. 1977, 25:441-444.
311. Valeur B. Molecular Fluorescence. Principles and Applications 2002, Wiley-VCH.
312. 138 in human lactoferrin: a study with glycosylation-site mutants. Biochemical Journal 1996, 319:117-122.
313. 1-acid glycoprotein (orosomucoid): pathophysiological changes in glycosylation in relation to its function. Glycoconjugate Journal 1995, 12:227-233.
314. Varriale L., Coppola E., Quarto M., Veneziani B.M., Palumbo G. Molecular aspects of photodynamic therapy: low energy pre-sensitization of hypericin-loaded human endometrial carcinoma cells enhances photo-tolerance alters gene expression and affects the cell cycle. FEBS Letters 2002, 512:287-290.
315. Vasquez G.B., Ji X., Fronticelli C., Gilliland G.L. Human carboxyhemoglobin at 2.2 resolution: structure and solvent comparisons of R-state, R2-state and T-state hemoglobins. Acta Crystallography D Biological Crystallography 1998, 54:355-366.
316. Verheyden S., Sillen A., Gils A., Declerck P.J., Engelborghs Y. Tryptophan properties in fluorescence and functional stability of plasminogen activator inhibitor 1. Biophysical Journal 2003, 85:501-510.
317. Vidugiris G.J.A., Royer C.A. Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states. Biophysical Journal 1998, 75:463-470.
318. Villette J.R., Helbecque N., Albani J.R., Sicard P.J., Bouquelet S.J. Cyclomaltodextrin glucanotransferase from Bacillus circulans E 192: nitration with tetranitromethane. Biotechnology and Applied Biochemistry 1993, 17:205-216.
319. 2 with micellar and monomeric inhibitors. A time-resolved fluorescence study of the tryptophan residue. European Journal of Biochemistry 1993, 215:531-539.
320. Wahl P., Weber G. Fluorescence depolarization of rabbit gamma globulin conjugates. Journal of Molecular Biology 1967, 30:371-382.
321. Ward D.C., Reich E., Stryer L. Fluorescence studies of nucleotides and polynucleotides. I. Formycin, 2-aminopurine riboside, 2,6-diaminopurine riboside, and their derivatives. Journal of Biological Chemistry 1969, 244:1228-1237.
322. Webb L.E., Fleischer E.B. Crystal structure of porphine. J. Chem. Phys. 1965, 43:3100-3111.
323. Weber G. Fluorescence of riboflavin and flavin-adenine dinucleotide. Biochemical Journal 1950, 47:114-121.
324. Weber G. Polarization of the fluorescence of macormolecules. I. Theory and experimental method. Biochemical Journal 1952, 51:145-155.
325. Weber G., Young L.B. Fragmentation of bovine serum albumin by pepsin. I. The origin of the acid expansion of the albumin molecule. Journal of Biological Chemistry 1964, 239:1415-1423.
326. Weber G., Farris F.G. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)naphthalene. Biochemistry 1979, 18:3075-3078.
327. Weber G. Order of free energy couplings between ligand binding and protein subunit association in hemoglobin. Proceedings of The Natural Academy of Sciences. U.S.A. 1984, 81:7098-7102.
328. Weber G., Scarlata S., Rholam M. Thermal coefficient of the frictional resistance to rotation in simple fluorophores determined by fluorescence polarization. Biochemistry 1984, 23:6785-6788.
329. Wetlaufer D.B. Ultraviolet absorptioni spectra of protens and amino acids, Advan. Protein Chem. 1962, 17:303-390.
330. Wrighton M.S., Ginley D.S., Morse D.L. A technique for the determination of absolute emission quantum yields of powdered samples. Journal of Physical Chemistry 1974, 78:2229-2233.
331. Wyss D.F., Wagner G. The structural role of sugars in glycoproteins. Current Opinions in Biotechnology 1996, 7:409-416.
332. 2 at 2.4 resolution. Journal of Molecular Biology 1990, 212:837-863.
333. Yang C.-C., Sklar P., Axel R., Maniatis A. Purification and characterization of a human RNA adenosine deaminase for glutamate receptor B pre-mRNA editing. Proceedings of The Naturl Academy of Sciences. U.S.A. 1997, 94:4354-4359.
334. Yi-Brunozzi H.Y., Stephens O.M., Beal P.A. Conformational changes that occur during an RNA-editing adenosine deami-nation reaction. Journal of Biological Chemistry 2001, 276:37827-37833.
335. York G.M., Walker G.C. The Rhizobium meliloti ExoK and ExsH glycanases specifically depolymerize nascent succinoglycan chains. Proceedings of The Natural Academy of Sciences. U.S.A. 1998, 95:4912-4917.
336. 1-Acid Glycoprotein, Age, and Sex in Mood Disorders. American Journal of Geriatric Psychiatry 1999, 7:331-334.
337. Yu P., Pettigrew D.W. Linkage between fructose 1,6-bisphosphate binding and the dimer-tetramer equilibrium of Escherichia coli glycerol kinase: critical behavior arising from change of ligand stoichiometry. Biochemistry 2003, 42:4243-4252.
338. Zandomeneghi M. Fluorescence of Cereal Flours. Journal of Agricultural and Food Chemistry 1999, 47:878-882.
339. Zandomeneghi M., Carbonaro L, Calucci L, Pinzino C, Galleschi L, Ghiringhelli S. Direct fluorometric determination of fluorescent substances in powders: the case of riboflavin in cereal fluors. Journal of Agricultural and Food Chemistry 2003, 51:2888-2895.
340. Zargarian L., Le Tilly V., Jamin N., Chaffotte A., Gabrielsen O.S., Toma F., Alpert B. Myb-DNA recognition: role of tryptophan residues and structural changes of the minimal DNA binding domain of c-Myb. Biochemistry 1999, 38:1921-1929.
341. Zentz C, Glandières J.M., El Moshni S., Alpert B. Protein matrix elasticity determined by fluorescence anisotropy of its tryptophan residues. Photochemistry and Photobiology 2003, 78:98-102.
342. Zhang M., Tanaka T., Ikura M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Structural Biology 1995, 2:758-767.