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Volumn 1844, Issue 3, 2014, Pages 576-584

FAD binding properties of a cytosolic version of Escherichia coli NADH dehydrogenase-2

Author keywords

FAD; Flavin binding; Flavoprotein; Fluorescence; NADH dehydrogenase

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE 2; UNCLASSIFIED DRUG;

EID: 84893061159     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.12.021     Document Type: Article
Times cited : (11)

References (52)
  • 1
    • 0032566696 scopus 로고    scopus 로고
    • Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology
    • DOI 10.1006/jmbi.1998.2045
    • E. Steensma, and C.P. van Mierlo Structural characterisation of apo-flavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology J. Mol. Biol. 282 1998 653 666 (Pubitemid 28428859)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.3 , pp. 653-666
    • Steensma, E.1    Van Mierlo, C.P.M.2
  • 2
    • 0015919686 scopus 로고
    • On the role of heme in the formation of the structure of cytochrome c
    • W.R. Fisher, H. Taniuchi, and C.B. Anfinsen On the role of heme in the formation of the structure of cytochrome c J. Biol. Chem. 248 1973 3188 3195
    • (1973) J. Biol. Chem. , vol.248 , pp. 3188-3195
    • Fisher, W.R.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 3
    • 0031952923 scopus 로고    scopus 로고
    • Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: Implications for redox potential regulation and flavodoxin folding
    • E. Steensma, M.J. Nijman, Y.J. Bollen, P.A. de Jager, W.A. van den Berg, W.M. van Dongen, and C.P. van Mierlo Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding Protein Sci. 7 1998 306 317 (Pubitemid 28092851)
    • (1998) Protein Science , vol.7 , Issue.2 , pp. 306-317
    • Steensma, E.1    Nijman, M.J.M.2    Bollen, Y.J.M.3    De Jager, P.A.4    Van Den Berg, W.A.M.5    Van Dongen, W.M.A.M.6    Van Mierlo, C.P.M.7
  • 5
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • DOI 10.1016/S0968-0004(99)01533-9, PII S0968000499015339
    • M.W. Fraaije, and A. Mattevi Flavoenzymes: diverse catalysts with recurrent features Trends Biochem. Sci. 25 2000 126 132 (Pubitemid 30122424)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.3 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 6
    • 0036919327 scopus 로고    scopus 로고
    • Flavoenzymes that catalyse reactions with no net redox change
    • DOI 10.1039/b108916c
    • S. Bornemann Flavoenzymes that catalyse reactions with no net redox change Nat. Prod. Rep. 19 2002 761 772 (Pubitemid 36029229)
    • (2002) Natural Product Reports , vol.19 , Issue.6 , pp. 761-772
    • Bornemann, S.1
  • 7
    • 34147109920 scopus 로고    scopus 로고
    • Linear array of conserved sequence motifs to discriminate protein subfamilies: Study on pyridine nucleotide-disulfide reductases
    • C.L. Ávila, V.A. Rapisarda, R.N. Farías, J. De Las Rivas, and R. Chehín Linear array of conserved sequence motifs to discriminate protein subfamilies: study on pyridine nucleotide-disulfide reductases BMC Bioinforma. 8 2007 96
    • (2007) BMC Bioinforma. , vol.8 , pp. 96
    • Ávila, C.L.1    Rapisarda, V.A.2    Farías, R.N.3    De Las Rivas, J.4    Chehín, R.5
  • 9
    • 0037022830 scopus 로고    scopus 로고
    • Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: Isolation and characterization
    • DOI 10.1021/bi015989w
    • J. Fang, and D.S. Beattie Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: isolation and characterization Biochemistry 41 2002 3065 3072 (Pubitemid 34184637)
    • (2002) Biochemistry , vol.41 , Issue.9 , pp. 3065-3072
    • Fang, J.1    Beattie, D.S.2
  • 10
    • 0142152465 scopus 로고    scopus 로고
    • Arabidopsis Genes Encoding Mitochondrial Type II NAD(P)H Dehydrogenases Have Different Evolutionary Origin and Show Distinct Responses to Light
    • DOI 10.1104/pp.103.024208
    • A.M. Michalecka, A.S. Svensson, F.I. Johansson, S.C. Agius, U. Johanson, A. Brennicke, S. Binder, and A.G. Rasmusson Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases have different evolutionary origin and show distinct responses to light Plant Physiol. 133 2003 642 652 (Pubitemid 37325676)
    • (2003) Plant Physiology , vol.133 , Issue.2 , pp. 642-652
    • Michalecka, A.M.1    Svensson, A.S.2    Johansson, F.I.3    Agius, S.C.4    Johanson, U.5    Brennicke, A.6    Binder, S.7    Rasmusson, A.G.8
  • 11
    • 79951975935 scopus 로고    scopus 로고
    • The mitochondrial respiratory chain
    • P.R. Rich, and A. Marechal The mitochondrial respiratory chain Essays Biochem. 47 2010 1 23
    • (2010) Essays Biochem. , vol.47 , pp. 1-23
    • Rich, P.R.1    Marechal, A.2
  • 13
    • 34250641971 scopus 로고    scopus 로고
    • The malaria parasite type II NADH:quinone oxidoreductase: An alternative enzyme for an alternative lifestyle
    • DOI 10.1016/j.pt.2007.04.014, PII S1471492207001158
    • N. Fisher, P.G. Bray, S.A. Ward, and G.A. Biagini The malaria parasite type II NADH:quinone oxidoreductase: an alternative enzyme for an alternative lifestyle Trends Parasitol. 23 2007 305 310 (Pubitemid 46935569)
    • (2007) Trends in Parasitology , vol.23 , Issue.7 , pp. 305-310
    • Fisher, N.1    Bray, P.G.2    Ward, S.A.3    Biagini, G.A.4
  • 16
    • 33744957049 scopus 로고    scopus 로고
    • Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis Type-II NADH-menaquinone oxidoreductase (NDH-2)
    • DOI 10.1074/jbc.M508844200
    • T. Yano, L.S. Li, E. Weinstein, J.S. Teh, and H. Rubin Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis type-II NADH-menaquinone oxidoreductase (NDH-2) J. Biol. Chem. 281 2006 11456 11463 (Pubitemid 43855400)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 11456-11463
    • Yano, T.1    Lin-Sheng, L.2    Weinstein, E.3    Teh, J.-S.4    Rubin, H.5
  • 17
    • 34547127139 scopus 로고    scopus 로고
    • Type II NADH:menaquinone oxidoreductase of Mycobacterium tuberculosis
    • J.S. Teh, T. Yano, and H. Rubin Type II NADH: menaquinone oxidoreductase of Mycobacterium tuberculosis Infect. Disord. Drug Targets 7 2007 169 181 (Pubitemid 47099126)
    • (2007) Infectious Disorders - Drug Targets , vol.7 , Issue.2 , pp. 169-181
    • Teh, J.S.1    Yano, T.2    Rubin, H.3
  • 18
    • 0034531991 scopus 로고    scopus 로고
    • Use of the NADH-quinone oxidoreductase (NDI1) gene of Saccharomyces cerevisiae as a possible cure for complex I defects in human cells
    • DOI 10.1074/jbc.M007033200
    • B.B. Seo, J. Wang, T.R. Flotte, T. Yagi, and A. Matsuno-Yagi Use of the NADH-quinone oxidoreductase (NDI1) gene of Saccharomyces cerevisiae as a possible cure for complex I defects in human cells J. Biol. Chem. 275 2000 37774 37778 (Pubitemid 32004893)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37774-37778
    • Seo, B.B.1    Wang, J.2    Flotte, T.R.3    Yagi, T.4    Matsuno-Yagi, A.5
  • 19
    • 77953082947 scopus 로고    scopus 로고
    • Molecular gene therapy: Overexpression of the alternative NADH dehydrogenase NDI1 restores overall physiology in a fungal model of respiratory complex i deficiency
    • M.F. Maas, C.H. Sellem, F. Krause, N.A. Dencher, and A. Sainsard-Chanet Molecular gene therapy: overexpression of the alternative NADH dehydrogenase NDI1 restores overall physiology in a fungal model of respiratory complex I deficiency J. Mol. Biol. 399 2010 31 40
    • (2010) J. Mol. Biol. , vol.399 , pp. 31-40
    • Maas, M.F.1    Sellem, C.H.2    Krause, F.3    Dencher, N.A.4    Sainsard-Chanet, A.5
  • 20
    • 80053439148 scopus 로고    scopus 로고
    • No immune responses by the expression of the yeast Ndi1 protein in rats
    • M. Marella, B.B. Seo, T.R. Flotte, A. Matsuno-Yagi, and T. Yagi No immune responses by the expression of the yeast Ndi1 protein in rats PLoS One 6 2011 25910
    • (2011) PLoS One , vol.6 , pp. 25910
    • Marella, M.1    Seo, B.B.2    Flotte, T.R.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 21
    • 76949106224 scopus 로고    scopus 로고
    • Parkinson's disease and mitochondrial complex I: A perspective on the Ndi1 therapy
    • M. Marella, B.B. Seo, T. Yagi, and A. Matsuno-Yagi Parkinson's disease and mitochondrial complex I: a perspective on the Ndi1 therapy J. Bioenerg. Biomembr. 41 2009 493 497
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 493-497
    • Marella, M.1    Seo, B.B.2    Yagi, T.3    Matsuno-Yagi, A.4
  • 22
    • 0019386665 scopus 로고
    • Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. UUG initiation codon
    • DOI 10.1111/j.1432-1033.1981.tb05314.x
    • I.G. Young, B.L. Rogers, H.D. Campbell, A. Jaworowski, and D.C. Shaw Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli: UUG initiation codon Eur. J. Biochem. 116 1981 165 170 (Pubitemid 11001652)
    • (1981) European Journal of Biochemistry , vol.116 , Issue.1 , pp. 165-170
    • Young, I.G.1    Rogers, B.L.2    Campbell, H.D.3
  • 23
    • 0019403472 scopus 로고
    • Characterization of the respiratory NADH dehydrogenase of Escherichia coli and reconstitution of NADH oxidase in ndh mutant membrane vesicles
    • DOI 10.1021/bi00515a049
    • A. Jaworowski, G. Mayo, D.C. Shaw, H.D. Campbell, and I.G. Young Characterization of the respiratory NADH dehydrogenase of Escherichia coli and reconstitution of NADH oxidase in ndh mutant membrane vesicles Biochemistry 20 1981 3621 3628 (Pubitemid 11058031)
    • (1981) Biochemistry , vol.20 , Issue.12 , pp. 3621-3628
    • Jaworowski, A.1    Mayo, G.2    Shaw, D.C.3
  • 25
    • 84866533591 scopus 로고    scopus 로고
    • The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates
    • M. Iwata, Y. Lee, T. Yamashita, T. Yagi, S. Iwata, A.D. Cameron, and M.J. Maher The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates Proc. Natl. Acad. Sci. U. S. A. 109 2012 15247 15252
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 15247-15252
    • Iwata, M.1    Lee, Y.2    Yamashita, T.3    Yagi, T.4    Iwata, S.5    Cameron, A.D.6    Maher, M.J.7
  • 26
    • 9644291930 scopus 로고    scopus 로고
    • Functional properties of the alternative NADH:ubiquinone oxidoreductase from E. Coli through comparative 3-D modelling
    • DOI 10.1016/j.febslet.2004.10.093, PII S0014579304013638
    • R. Schmid, and D.L. Gerloff Functional properties of the alternative NADH: ubiquinone oxidoreductase from E. coli through comparative 3-D modeling FEBS Lett. 578 2004 163 168 (Pubitemid 39576119)
    • (2004) FEBS Letters , vol.578 , Issue.1-2 , pp. 163-168
    • Schmid, R.1    Gerloff, D.L.2
  • 27
    • 0036718981 scopus 로고    scopus 로고
    • Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2
    • DOI 10.1016/S0003-9861(02)00277-1, PII S0003986102002771
    • V.A. Rapisarda, R.N. Chehín, J. De Las Rivas, L. Rodríguez-Montelongo, R.N. Farías, and E.M. Massa Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2 Arch. Biochem. Biophys. 405 2002 87 94 (Pubitemid 35026170)
    • (2002) Archives of Biochemistry and Biophysics , vol.405 , Issue.1 , pp. 87-94
    • Rapisarda, V.A.1    Chehin, R.N.2    De Las Rivas, J.3    Rodriguez-Montelongo, L.4    Farias, R.N.5    Massa, E.M.6
  • 28
    • 78651258376 scopus 로고    scopus 로고
    • Amphipathic C-terminal region of Escherichia coli NADH dehydrogenase-2 mediates membrane localization
    • J.M. Villegas, S.I. Volentini, M.R. Rintoul, and V.A. Rapisarda Amphipathic C-terminal region of Escherichia coli NADH dehydrogenase-2 mediates membrane localization Arch. Biochem. Biophys. 505 2011 155 159
    • (2011) Arch. Biochem. Biophys. , vol.505 , pp. 155-159
    • Villegas, J.M.1    Volentini, S.I.2    Rintoul, M.R.3    Rapisarda, V.A.4
  • 30
    • 0025265852 scopus 로고
    • Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints
    • G. Eggink, H. Engel, G. Vriend, P. Terpstra, and B. Witholt Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints J. Mol. Biol. 212 1990 135 142
    • (1990) J. Mol. Biol. , vol.212 , pp. 135-142
    • Eggink, G.1    Engel, H.2    Vriend, G.3    Terpstra, P.4    Witholt, B.5
  • 31
    • 0345151821 scopus 로고    scopus 로고
    • Characterization of an NADH-linked cupric reductase activity from the Escherichia coli respiratory chain
    • DOI 10.1006/abbi.1999.1398
    • V.A. Rapisarda, L.R. Montelongo, R.N. Farías, and E.M. Massa Characterization of an NADH-linked cupric reductase activity from the Escherichia coli respiratory chain Arch. Biochem. Biophys. 370 1999 143 150 (Pubitemid 29491418)
    • (1999) Archives of Biochemistry and Biophysics , vol.370 , Issue.2 , pp. 143-150
    • Rapisarda, V.A.1    Montelongo, L.R.2    Farias, R.N.3    Massa, E.M.4
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 84864699707 scopus 로고    scopus 로고
    • Hydrogen-bonding modulation of excited-state properties of flavins in a model of aqueous confined environment
    • L. Valle, F.E.M. Vieyra, and C.D. Borsarelli Hydrogen-bonding modulation of excited-state properties of flavins in a model of aqueous confined environment Photochem. Photobiol. Sci. 11 2012 1051 1061
    • (2012) Photochem. Photobiol. Sci. , vol.11 , pp. 1051-1061
    • Valle, L.1    Vieyra, F.E.M.2    Borsarelli, C.D.3
  • 38
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • DOI 10.1016/j.ab.2006.07.027, PII S0003269706005355
    • U.B. Ericsson, B.M. Hallberg, G.T. DeTitta, N. Dekker, and P. Nordlund Thermofluor-based high-throughput stability optimization of proteins for structural studies Anal. Biochem. 357 2006 289 298 (Pubitemid 44430091)
    • (2006) Analytical Biochemistry , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 39
    • 0025611286 scopus 로고
    • Characterization of a fully active N-terminal 37-kDa polypeptide obtained by limited tryptic cleavage of pig kidney D-amino acid oxidase
    • G.T. Tarelli, M.A. Vanoni, A. Negri, and B. Curti Characterization of a fully active N-terminal 37-kDa polypeptide obtained by limited tryptic cleavage of pig kidney D-amino acid oxidase J. Biol. Chem. 265 1990 21242 21246 (Pubitemid 120014145)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.34 , pp. 21242-21246
    • Tarelli, G.T.1    Vanoni, M.A.2    Negri, A.3    Curti, B.4
  • 41
    • 0034711283 scopus 로고    scopus 로고
    • FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli
    • DOI 10.1074/jbc.M004777200
    • H. Lindsay, E. Beaumont, S.D. Richards, S.M. Kelly, S.J. Sanderson, N.C. Price, and J.G. Lindsay FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli J. Biol. Chem. 275 2000 36665 36670 (Pubitemid 32002069)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 36665-36670
    • Lindsay, H.1    Beaumont, E.2    Richards, S.D.3    Kelly, S.M.4    Sanderson, S.J.5    Price, N.C.6    Lindsay, J.G.7
  • 42
    • 0035909813 scopus 로고    scopus 로고
    • Apoflavodoxin folding mechanism: An α/β protein with an essentially off-pathway intermediate
    • DOI 10.1021/bi010216t
    • J. Fernández-Recio, C.G. Genzor, and J. Sancho Apoflavodoxin folding mechanism: an alpha/beta protein with an essentially off-pathway intermediate Biochemistry 40 2001 15234 15245 (Pubitemid 33151938)
    • (2001) Biochemistry , vol.40 , Issue.50 , pp. 15234-15245
    • Fernandez-Recio, J.1    Genzor, C.G.2    Sancho, J.3
  • 43
    • 4043074820 scopus 로고    scopus 로고
    • Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin
    • DOI 10.1021/bi049545m
    • Y.J. Bollen, I.E. Sánchez, and C.P. van Mierlo Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin Biochemistry 43 2004 10475 10489 (Pubitemid 39079320)
    • (2004) Biochemistry , vol.43 , Issue.32 , pp. 10475-10489
    • Bollen, Y.J.M.1    Sanchez, I.E.2    Van Mierlo, C.P.M.3
  • 45
    • 79953678110 scopus 로고    scopus 로고
    • Modulation of the photocycle of a LOV domain photoreceptor by hydrogen-bonding network
    • S. Raffelberg, M. Mansurova, W. Gärtner, and A. Losi Modulation of the photocycle of a LOV domain photoreceptor by hydrogen-bonding network J. Am. Chem. Soc. 113 2011 5346 5356
    • (2011) J. Am. Chem. Soc. , vol.113 , pp. 5346-5356
    • Raffelberg, S.1    Mansurova, M.2    Gärtner, W.3    Losi, A.4
  • 46
    • 34547681744 scopus 로고    scopus 로고
    • Steady-state fluorescence anisotropy to investigate flavonoids binding to proteins
    • C.M. Ingersoll, and C.M. Strollo Steady-state fluorescence anisotropy to investigate flavonoids binding to proteins J. Chem. Educ. 84 2007 1313 1315 (Pubitemid 47208715)
    • (2007) Journal of Chemical Education , vol.84 , Issue.8 , pp. 1313-1315
    • Ingersoll, C.M.1    Strollo, C.M.2
  • 47
    • 1842424838 scopus 로고    scopus 로고
    • Structural Studies on Flavin Reductase PheA2 Reveal Binding of NAD in an Unusual Folded Conformation and Support Novel Mechanism of Action
    • DOI 10.1074/jbc.M313765200
    • R.H. van den Heuvel, A.H. Westphal, A.J. Heck, M.A. Walsh, S. Rovida, W.J. van Berkel, and A. Mattevi Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action J. Biol. Chem. 279 2004 12860 12867 (Pubitemid 38445860)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12860-12867
    • Van Den Heuvel, R.H.H.1    Westphal, A.H.2    Heck, A.J.R.3    Walsh, M.A.4    Rovida, S.5    Van Berkel, W.J.H.6    Mattevi, A.7
  • 48
    • 67650066652 scopus 로고    scopus 로고
    • The role of adenine in fast excited-state deactivation of FAD: A femtosecond mid-IR transient absorption study
    • G.F. Li, and K.D. Glusac The role of adenine in fast excited-state deactivation of FAD: a femtosecond mid-IR transient absorption study J. Phys. Chem. B 113 2009 9059 9061
    • (2009) J. Phys. Chem. B , vol.113 , pp. 9059-9061
    • Li, G.F.1    Glusac, K.D.2
  • 49
    • 84155167320 scopus 로고    scopus 로고
    • Evaluation of solute binding to proteins and intra-protein distances from steady state fluorescence measurements
    • E. Alarcón, A. Aspée, E.B. Abuin, and E.A. Lissi Evaluation of solute binding to proteins and intra-protein distances from steady state fluorescence measurements J. Photochem. Photobiol. B Biol. 106 2012 1 17
    • (2012) J. Photochem. Photobiol. B Biol. , vol.106 , pp. 1-17
    • Alarcón, E.1    Aspée, A.2    Abuin, E.B.3    Lissi, E.A.4
  • 50
    • 0021276526 scopus 로고
    • Peptide binding by calmodulin and its proteolytic fragments and by troponin C
    • D.A. Malencik, and S.R. Anderson Peptide binding by calmodulin and its proteolytic fragments and by troponin-C Biochemistry 23 1984 2420 2428 (Pubitemid 14113662)
    • (1984) Biochemistry , vol.23 , Issue.11 , pp. 2420-2428
    • Malencik, D.A.1    Anderson, S.R.2
  • 51
    • 0035860106 scopus 로고    scopus 로고
    • The analysis of time resolved protein fluorescence in multi-tryptophan proteins
    • DOI 10.1016/S1386-1425(01)00485-1, PII S1386142501004851
    • Y. Engelborghs The analysis of time resolved protein fluorescence in multi-tryptophan proteins Spectrochim. Acta A Mol. Biomol. Spectrosc. 57 2001 2255 2270 (Pubitemid 32867025)
    • (2001) Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy , vol.57 , Issue.11 , pp. 2255-2270
    • Engelborghs, Y.1
  • 52
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • M. van de Weert, and L. Stella Fluorescence quenching and ligand binding: a critical discussion of a popular methodology J. Mol. Struct. 998 2011 144 150
    • (2011) J. Mol. Struct. , vol.998 , pp. 144-150
    • Van De Weert, M.1    Stella, L.2


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