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Volumn 12, Issue 9, 2003, Pages 2104-2108

Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c

Author keywords

G tensor; Hyperfine shifts; Labeling hemeproteins; NMR resonance assignments; Paramagnetic shifts

Indexed keywords

CYTOCHROME C;

EID: 0042510863     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03211303     Document Type: Article
Times cited : (26)

References (25)
  • 1
    • 44949288628 scopus 로고
    • Proton-proton correlation via isotropic mixing of carbon-13 magnetization, a new three-dimensional approach for assigning proton and carbon-13 spectra of carbon-13-enriched proteins
    • Bax, A., Clore, G.M., and Gronenborn, A.M. 1990. Proton-proton correlation via isotropic mixing of carbon-13 magnetization, a new three-dimensional approach for assigning proton and carbon-13 spectra of carbon-13-enriched proteins. J. Magn. Reson. 88: 425-431.
    • (1990) J. Magn. Reson. , vol.88 , pp. 425-431
    • Bax, A.1    Clore, G.M.2    Gronenborn, A.M.3
  • 2
    • 0026608669 scopus 로고
    • Oxidation state-dependent conformational changes in cytochrome c
    • Berghuis, A.W. and Brayer, G.D. 1992. Oxidation state-dependent conformational changes in cytochrome c. J. Mol. Biol. 223: 959-976.
    • (1992) J. Mol. Biol. , vol.223 , pp. 959-976
    • Berghuis, A.W.1    Brayer, G.D.2
  • 3
    • 0038188962 scopus 로고    scopus 로고
    • Paramagnetic constraints: An aid for quick solution structure determination of paramagnetic metalloproteins
    • Bertini, I., Luchinat, C., and Parigi. G. 2002. Paramagnetic constraints: An aid for quick solution structure determination of paramagnetic metalloproteins. Concept. Magn. Res. 14: 259-286.
    • (2002) Concept. Magn. Res. , vol.14 , pp. 259-286
    • Bertini, I.1    Luchinat, C.2    Parigi, G.3
  • 6
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander, S.W. 2001. Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct. 29: 213-238.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 8
    • 0025234717 scopus 로고
    • Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c
    • Feng, Y., Roder, H., and Englander, S.W. 1990. Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c. Biochemistry 29: 3494-3504.
    • (1990) Biochemistry , vol.29 , pp. 3494-3504
    • Feng, Y.1    Roder, H.2    Englander, S.W.3
  • 9
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S. and Bax, A. 1992. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114: 6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 10
    • 0015803280 scopus 로고
    • Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems. Ferricytochrome c and metmyoglobin cyanide
    • Horrocks Jr., W.D. and Greenberg, S. 1973. Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems. Ferricytochrome c and metmyoglobin cyanide. Biochim. Biophys. Acta 322: 38-44.
    • (1973) Biochim. Biophys. Acta , vol.322 , pp. 38-44
    • Horrocks W.D., Jr.1    Greenberg, S.2
  • 11
    • 0036963585 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human cytochrome c in E. coli
    • Jeng, W.-Y., Chen, C.-Y., Chang, H.-C., and Chuang, W.-J. 2002. Expression and characterization of recombinant human cytochrome c in E. coli. J. Bioenerg. Biomemb. 34: 423-431.
    • (2002) J. Bioenerg. Biomemb. , vol.34 , pp. 423-431
    • Jeng, W.-Y.1    Chen, C.-Y.2    Chang, H.-C.3    Chuang, W.-J.4
  • 12
    • 0001018129 scopus 로고
    • Isotropic NMR shifts in transition metal complexes: Calculation of the Fermi contact and pseudocontact terms
    • Kurland, R.J. and McGarvey, B.R.J. 1970. Isotropic NMR shifts in transition metal complexes: Calculation of the Fermi contact and pseudocontact terms. J. Magn. Reson. 2: 286-301.
    • (1970) J. Magn. Reson. , vol.2 , pp. 286-301
    • Kurland, R.J.1    McGarvey, B.R.J.2
  • 13
    • 0035846624 scopus 로고    scopus 로고
    • Main chain and side chain dynamics of oxidized flavodoxin from Cyanobacterium anabaena
    • Liu, W., Flynn, P.F., Fuentes, E.J., Kranz, J.K., McCormick, M., and Wand, A.J. 2001. Main chain and side chain dynamics of oxidized flavodoxin from Cyanobacterium anabaena. Biochemistry 40: 14744-14753.
    • (2001) Biochemistry , vol.40 , pp. 14744-14753
    • Liu, W.1    Flynn, P.F.2    Fuentes, E.J.3    Kranz, J.K.4    McCormick, M.5    Wand, A.J.6
  • 14
    • 0037184910 scopus 로고    scopus 로고
    • Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis
    • Martin, A.G. and Fearnhead, H.O. 2002. Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis. J. Biol. Chem. 277: 50834-50841.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50834-50841
    • Martin, A.G.1    Fearnhead, H.O.2
  • 15
    • 84890928276 scopus 로고
    • An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins
    • Montelione, G.T., Lyons, B.A., Emerson, S.D., and Tashiro, M. 1992. An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins. J. Am. Chem. Soc. 114: 10974-10975.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10974-10975
    • Montelione, G.T.1    Lyons, B.A.2    Emerson, S.D.3    Tashiro, M.4
  • 17
    • 0024435833 scopus 로고
    • Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling
    • Neri, D., Szyperski, T., Otting, G., Senn, H., and Wüthrich, K. 1989. Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling. Biochemistry 28: 7510-7516.
    • (1989) Biochemistry , vol.28 , pp. 7510-7516
    • Neri, D.1    Szyperski, T.2    Otting, G.3    Senn, H.4    Wüthrich, K.5
  • 18
    • 0034957675 scopus 로고    scopus 로고
    • Characterization of horse cytochrome c expressed in Escherichia coli
    • Patel, C.N., Lind, M.C., and Pielak, G.J. 2001. Characterization of horse cytochrome c expressed in Escherichia coli. Protein Expr. Purif. 22: 220-224.
    • (2001) Protein Expr. Purif. , vol.22 , pp. 220-224
    • Patel, C.N.1    Lind, M.C.2    Pielak, G.J.3
  • 19
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • Pollock, W.B.R., Rosell, F.I., Twitchett, M.B., Dumont, M.E., and Mauk, A.G. 1998. Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry 37: 6124-6131.
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.R.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 20
    • 0037180383 scopus 로고    scopus 로고
    • Recombinant equine cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants
    • Rumbley, J.N., Hoang, L., and Englander, S.W, 2002. Recombinant equine cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants. Biochemistry 41: 13894-13901.
    • (2002) Biochemistry , vol.41 , pp. 13894-13901
    • Rumbley, J.N.1    Hoang, L.2    Englander, S.W.3
  • 25
    • 43949167657 scopus 로고
    • HNCACB, A high sensitivity 3D NMR experiment to correlate amide proton and nitrogen resonances with the α-carbon and β-carbon resonances in proteins
    • Wittekind, M. and Mueller, L. 1993. HNCACB, A high sensitivity 3D NMR experiment to correlate amide proton and nitrogen resonances with the α-carbon and β-carbon resonances in proteins. J. Magn. Reson. 101B: 201-205.
    • (1993) J. Magn. Reson. , vol.101 B , pp. 201-205
    • Wittekind, M.1    Mueller, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.