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Volumn 72, Issue 1, 2008, Pages 34-40

Tyrosine side chains as an electrochemical probe of stacked β-sheet protein conformations

Author keywords

Amyloids; Differential pulse voltammetry; Electrochemistry; Polyaminoacids; Tyrosine

Indexed keywords

CONFORMATIONS; CYCLIC VOLTAMMETRY; DISEASES; ELECTROCHEMISTRY; MOLECULAR STRUCTURE; MONOMERS; POLYPEPTIDES;

EID: 38749117884     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2007.07.004     Document Type: Article
Times cited : (23)

References (38)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: the importance of being unfolded
    • Uversky V.N., and Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698 (2004) 131-153
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 3
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich M., Fletcher M.A., and Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature 410 (2001) 165-166
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 4
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien P., Weissman J.S., and DePace A.H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73 (2004) 617-656
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 6
    • 1642299396 scopus 로고    scopus 로고
    • The diastereomeric assembly of polylysine is the low-volume pathway for preferential formation of β-sheet aggregates
    • Dzwolak W., Ravindra R., Nicolini C., Jansen R., and Winter R.J. The diastereomeric assembly of polylysine is the low-volume pathway for preferential formation of β-sheet aggregates. J. Am. Chem. Soc. 126 (2004) 3762-3768
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3762-3768
    • Dzwolak, W.1    Ravindra, R.2    Nicolini, C.3    Jansen, R.4    Winter, R.J.5
  • 7
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
    • Jansen R., Dzwolak W., and Winter R. Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy. Biophys. J. 88 (2005) 1344-1353
    • (2005) Biophys. J. , vol.88 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 8
    • 3042665537 scopus 로고    scopus 로고
    • Insulin forms amyloid in a strain-dependent manner: an FTIR spectroscopy study
    • Dzwolak W., Smirnovas V., Jansen R., and Winter R. Insulin forms amyloid in a strain-dependent manner: an FTIR spectroscopy study. Prot. Sci. 13 (2004) 1927-1932
    • (2004) Prot. Sci. , vol.13 , pp. 1927-1932
    • Dzwolak, W.1    Smirnovas, V.2    Jansen, R.3    Winter, R.4
  • 9
    • 0025101761 scopus 로고
    • Protective effect of lipid surfaces against pressure-induced conformational changes of poly(l-lysine)
    • Carrier D., Mantsch H.H., and Wong P.T.T. Protective effect of lipid surfaces against pressure-induced conformational changes of poly(l-lysine). Biochemistry 29 (1990) 254-258
    • (1990) Biochemistry , vol.29 , pp. 254-258
    • Carrier, D.1    Mantsch, H.H.2    Wong, P.T.T.3
  • 10
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth A. The infrared absorption of amino acid side chains. Prog. Biophys. Mol. Biol. 74 (2000) 141-173
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 141-173
    • Barth, A.1
  • 11
    • 16544387870 scopus 로고    scopus 로고
    • The electrochemical behavior and amperometric determination of tyrosine and tryptophan at a glassy carbon electrode modified with butyrylcholine
    • Guang-Ping J., and Xiang-Qin L. The electrochemical behavior and amperometric determination of tyrosine and tryptophan at a glassy carbon electrode modified with butyrylcholine. Electrochem. Commun. 6 (2004) 454-460
    • (2004) Electrochem. Commun. , vol.6 , pp. 454-460
    • Guang-Ping, J.1    Xiang-Qin, L.2
  • 12
    • 7744239249 scopus 로고
    • Further comments on the redox potentials of tryptophan and tyrosine
    • Harriman A.J. Further comments on the redox potentials of tryptophan and tyrosine. J. Phys. Chem. 91 (1987) 6102-6104
    • (1987) J. Phys. Chem. , vol.91 , pp. 6102-6104
    • Harriman, A.J.1
  • 13
    • 0031805374 scopus 로고    scopus 로고
    • Tyrosine confounds oxidative electrochemical detection of nitric oxide
    • Stingele R., Wilson D.A., Traytstman R.J., and Hanley D.F. Tyrosine confounds oxidative electrochemical detection of nitric oxide. Am. J. Physiol. 274 (1998) 1698-1704
    • (1998) Am. J. Physiol. , vol.274 , pp. 1698-1704
    • Stingele, R.1    Wilson, D.A.2    Traytstman, R.J.3    Hanley, D.F.4
  • 14
    • 49149145521 scopus 로고
    • Electrochemical oxidation of nucleic acids and proteins at graphite electrode. Qualitative aspects
    • Brabec V. Electrochemical oxidation of nucleic acids and proteins at graphite electrode. Qualitative aspects. Bioelectrochem. Bioenerg. 7 (1980) 69-82
    • (1980) Bioelectrochem. Bioenerg. , vol.7 , pp. 69-82
    • Brabec, V.1
  • 15
    • 0030579065 scopus 로고    scopus 로고
    • Potentiometric stripping analysis of bioactive peptides at carbon electrodes down to subnanomolar concentrations
    • Cai X., Rivas G., Farias P., Shiraishi H., Wang J., and Palecek E. Potentiometric stripping analysis of bioactive peptides at carbon electrodes down to subnanomolar concentrations. Anal. Chim. Acta 332 (1996) 49-57
    • (1996) Anal. Chim. Acta , vol.332 , pp. 49-57
    • Cai, X.1    Rivas, G.2    Farias, P.3    Shiraishi, H.4    Wang, J.5    Palecek, E.6
  • 16
    • 24144437434 scopus 로고    scopus 로고
    • A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid beta aggregation
    • Vestergaard M., Kerman K., Saito M., Nagatani N., Takamura Y., and Tamiya E. A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid beta aggregation. J. Am. Chem. Soc. 127 (2005) 11892-11893
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11892-11893
    • Vestergaard, M.1    Kerman, K.2    Saito, M.3    Nagatani, N.4    Takamura, Y.5    Tamiya, E.6
  • 17
    • 38749133072 scopus 로고
    • Polarographic determination of phenylalanine, tyrosine, methionine, glutamic acid and histidine with a dropping copper amalgam electrode
    • Sanchez Perez A., and Lucena Conde F.J. Polarographic determination of phenylalanine, tyrosine, methionine, glutamic acid and histidine with a dropping copper amalgam electrode. J. Electroanal. Chem. 74 (1976) 339-346
    • (1976) J. Electroanal. Chem. , vol.74 , pp. 339-346
    • Sanchez Perez, A.1    Lucena Conde, F.J.2
  • 18
    • 0030703007 scopus 로고    scopus 로고
    • Electrochemical oxidation reactions of tyrosine, tryptophan and related dipeptides
    • MacDonald S.M., and Roscoe S.G. Electrochemical oxidation reactions of tyrosine, tryptophan and related dipeptides. Electrochim. Acta 42 (1997) 1189-1200
    • (1997) Electrochim. Acta , vol.42 , pp. 1189-1200
    • MacDonald, S.M.1    Roscoe, S.G.2
  • 19
    • 27744465635 scopus 로고    scopus 로고
    • FTIR studies of tyrosine oxidation at polycrystalline Pt and Pt (111) electrodes
    • Zinola C.F., Rodrigues J.L., Arevalo M.C., and Pastor E.J. FTIR studies of tyrosine oxidation at polycrystalline Pt and Pt (111) electrodes. J. Electroanal. Chem. 585 (2005) 230-239
    • (2005) J. Electroanal. Chem. , vol.585 , pp. 230-239
    • Zinola, C.F.1    Rodrigues, J.L.2    Arevalo, M.C.3    Pastor, E.J.4
  • 20
    • 0344241149 scopus 로고    scopus 로고
    • In-situ FTIR studies on the electrochemial oxidation of histidine and tyrosine
    • Ogura K., Kobayashi M., Nakayama M., and Miho Y.J. In-situ FTIR studies on the electrochemial oxidation of histidine and tyrosine. J. Electroanal. Chem. 463 (1999) 218-223
    • (1999) J. Electroanal. Chem. , vol.463 , pp. 218-223
    • Ogura, K.1    Kobayashi, M.2    Nakayama, M.3    Miho, Y.J.4
  • 21
    • 0006160112 scopus 로고
    • Electrochemical investigations of amino acids at solid electrodes. Part II: amino acids containing no sulfur atoms: tryptophan, tyrosine, histidine and derivatives
    • Malfoy B., and Reynaud J.A. Electrochemical investigations of amino acids at solid electrodes. Part II: amino acids containing no sulfur atoms: tryptophan, tyrosine, histidine and derivatives. J. Electroanal. Chem 114 (1980) 213-223
    • (1980) J. Electroanal. Chem , vol.114 , pp. 213-223
    • Malfoy, B.1    Reynaud, J.A.2
  • 22
    • 0000577514 scopus 로고
    • The electrochemical oxidation of three proteins: RNAase A, bovine serum albumine and concanavalin A at solid electrodes
    • Reynaud J.A., Malfoy B., and Bere A. The electrochemical oxidation of three proteins: RNAase A, bovine serum albumine and concanavalin A at solid electrodes. Bioelectrochem. Bioenerg. 7 (1980) 595-606
    • (1980) Bioelectrochem. Bioenerg. , vol.7 , pp. 595-606
    • Reynaud, J.A.1    Malfoy, B.2    Bere, A.3
  • 23
    • 0000459574 scopus 로고
    • Anodic oxidation pathways of phenolic compounds. Part I: anodic hydroxylation reactions
    • Papouchado L., Petrie G., and Adams R.N. Anodic oxidation pathways of phenolic compounds. Part I: anodic hydroxylation reactions. Electroanal. Chem. Interfac. Chem. 38 (1972) 389-395
    • (1972) Electroanal. Chem. Interfac. Chem. , vol.38 , pp. 389-395
    • Papouchado, L.1    Petrie, G.2    Adams, R.N.3
  • 24
    • 0000163844 scopus 로고
    • Indirect electrochemical determination of l-tyrosine using mushroom tyrosinase in solution
    • Rivas G.A., and Solis V.M. Indirect electrochemical determination of l-tyrosine using mushroom tyrosinase in solution. Anal. Chem. 63 (1991) 2762-2765
    • (1991) Anal. Chem. , vol.63 , pp. 2762-2765
    • Rivas, G.A.1    Solis, V.M.2
  • 25
    • 11144251132 scopus 로고    scopus 로고
    • Kinetic study of the oxidation of some catecholamines by digital simulation of cyclic voltammograms
    • Afkhami A., Nematollahi D., Khalafi L., and Rafiee M. Kinetic study of the oxidation of some catecholamines by digital simulation of cyclic voltammograms. Int. J. Chem. Kinet. 37 (2005) 17-24
    • (2005) Int. J. Chem. Kinet. , vol.37 , pp. 17-24
    • Afkhami, A.1    Nematollahi, D.2    Khalafi, L.3    Rafiee, M.4
  • 26
    • 16344378453 scopus 로고    scopus 로고
    • Development of a sensor based on tetracyanoethylenide (LiTCNE)/poly-l-lysine (FILL) for dopamine determination
    • Luz R., Damos F.Z., Oliveira A., Beck J., and Kubota L.T. Development of a sensor based on tetracyanoethylenide (LiTCNE)/poly-l-lysine (FILL) for dopamine determination. Electrochim. Acta 50 (2005) 2675-2683
    • (2005) Electrochim. Acta , vol.50 , pp. 2675-2683
    • Luz, R.1    Damos, F.Z.2    Oliveira, A.3    Beck, J.4    Kubota, L.T.5
  • 27
    • 84987492787 scopus 로고
    • The voltammetry of neuropeptides containing l-tyrosine
    • Reynolds N.C., Kissela B.M., and Fleming L.H. The voltammetry of neuropeptides containing l-tyrosine. Electroanalysis 7 (1995) 1177-1181
    • (1995) Electroanalysis , vol.7 , pp. 1177-1181
    • Reynolds, N.C.1    Kissela, B.M.2    Fleming, L.H.3
  • 28
    • 0037292933 scopus 로고    scopus 로고
    • Spectroelectrochemical and voltammetric studies of l-DOPA
    • Liu X., Zhang Z., Cheng G., and Dong S. Spectroelectrochemical and voltammetric studies of l-DOPA. Electroanalysis 15 (2003) 103-107
    • (2003) Electroanalysis , vol.15 , pp. 103-107
    • Liu, X.1    Zhang, Z.2    Cheng, G.3    Dong, S.4
  • 29
  • 30
    • 0012682721 scopus 로고    scopus 로고
    • Anodic oxidation of oxygen-containing compounds
    • Lund M., and Hammerich O. (Eds), Marcel Dekker, New York
    • Morrow G.W. Anodic oxidation of oxygen-containing compounds. In: Lund M., and Hammerich O. (Eds). Organic Electrochemistry. 4th ed. (2002), Marcel Dekker, New York 589-618
    • (2002) Organic Electrochemistry. 4th ed. , pp. 589-618
    • Morrow, G.W.1
  • 31
    • 0037024435 scopus 로고    scopus 로고
    • Electrooxidation of 2,4-dichlorophenol and other polychlorinated phenols at glassy carbon electrode
    • Ureta-Zanartu M.S., Bustos P., Berros C., Diez M.C., Mora M.L., and Gutierrez C. Electrooxidation of 2,4-dichlorophenol and other polychlorinated phenols at glassy carbon electrode. Electrochim. Acta 47 (2002) 2399-2406
    • (2002) Electrochim. Acta , vol.47 , pp. 2399-2406
    • Ureta-Zanartu, M.S.1    Bustos, P.2    Berros, C.3    Diez, M.C.4    Mora, M.L.5    Gutierrez, C.6
  • 34
    • 0030218327 scopus 로고    scopus 로고
    • Electrochemical assay and properties of plasmin adsorbed onto a carbon paste electrode
    • Longchamp S., Randriamabazaka N., and Nigretto J.M. Electrochemical assay and properties of plasmin adsorbed onto a carbon paste electrode. J. Electroanal. Chem. 412 (1996) 31-37
    • (1996) J. Electroanal. Chem. , vol.412 , pp. 31-37
    • Longchamp, S.1    Randriamabazaka, N.2    Nigretto, J.M.3
  • 35
    • 33845283486 scopus 로고
    • Oxidation chemistry of 5-hydroxytryptamine. 1. Mechanism and products formed at micromolar concentrations
    • Wrona M.Z., and Dryhurst G.J. Oxidation chemistry of 5-hydroxytryptamine. 1. Mechanism and products formed at micromolar concentrations. Org. Chem. 52 (1987) 2817-2825
    • (1987) Org. Chem. , vol.52 , pp. 2817-2825
    • Wrona, M.Z.1    Dryhurst, G.J.2
  • 36
    • 0034038196 scopus 로고    scopus 로고
    • Electrochemical oxidation of histamine and serotonin at highly boron-doped diamond electrodes
    • Sarada B.V., Rao T.N., Tryk D.A., and Fujishima A. Electrochemical oxidation of histamine and serotonin at highly boron-doped diamond electrodes. Anal. Chem. 72 (2000) 1632-1638
    • (2000) Anal. Chem. , vol.72 , pp. 1632-1638
    • Sarada, B.V.1    Rao, T.N.2    Tryk, D.A.3    Fujishima, A.4
  • 37
    • 0021213448 scopus 로고
    • Oxidation of tyrosine residues in proteins by tyrosinase
    • Ito S., Kato T., Shinpo K., and Fujita K. Oxidation of tyrosine residues in proteins by tyrosinase. Biochem. J. 222 (1984) 407-411
    • (1984) Biochem. J. , vol.222 , pp. 407-411
    • Ito, S.1    Kato, T.2    Shinpo, K.3    Fujita, K.4
  • 38
    • 0032310799 scopus 로고    scopus 로고
    • Characterisation of electrosynthetic L-dopa-melanin films by electrochemical and spectroelectrochemical techniques
    • Robinson G.M., Iwuocha E.I., and Smyth M.R. Characterisation of electrosynthetic L-dopa-melanin films by electrochemical and spectroelectrochemical techniques. Electrochim. Acta 43 (1998) 3489-3496
    • (1998) Electrochim. Acta , vol.43 , pp. 3489-3496
    • Robinson, G.M.1    Iwuocha, E.I.2    Smyth, M.R.3


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