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Volumn 46, Issue 45, 2007, Pages 13120-13130

Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin α: Evidence for metalation as an entropic switch

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; CELL PROLIFERATION; ELECTROSPRAY IONIZATION; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATIVE STRESS; ZINC;

EID: 36048990877     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7014822     Document Type: Article
Times cited : (52)

References (90)
  • 1
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm, J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 3
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002) Intrinsically unstructured proteins, Trends Biochem. Sci. 27, 527-533.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 4
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J., and Wright, P. E. (2005) Intrinsically unstructured proteins and their functions, Nat. Rev. Mol. Cell. Biol. 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell. Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 5
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa, P. (2005) The interplay between structure and function in intrinsically unstructured proteins, FEBS Lett. 579, 3346-3354.
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 6
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., and Jones, D. T. (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life, J. Mol. Biol. 337, 635-645.
    • (2004) J. Mol. Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 8
    • 33748280715 scopus 로고    scopus 로고
    • Abundance of intrinsic disorder in protein associated with cardiovascular disease
    • Cheng, Y., LeGall, T., Oldfield, C. J., Dunker, A. K., and Uversky, V. N. (2006) Abundance of intrinsic disorder in protein associated with cardiovascular disease, Biochemistry 45, 10448-10460.
    • (2006) Biochemistry , vol.45 , pp. 10448-10460
    • Cheng, Y.1    LeGall, T.2    Oldfield, C.J.3    Dunker, A.K.4    Uversky, V.N.5
  • 9
    • 33744829805 scopus 로고    scopus 로고
    • Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation
    • Minezaki, Y., Homma, K., Kinjo, A. R., and Nishikawa, K. (2006) Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation, J. Mol. Biol. 359, 1137-1149.
    • (2006) J. Mol. Biol , vol.359 , pp. 1137-1149
    • Minezaki, Y.1    Homma, K.2    Kinjo, A.R.3    Nishikawa, K.4
  • 11
    • 0034912536 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states
    • Dyson, H. J., and Wright, P. E. (2001) Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states, Methods Enzymol. 339, 258-270.
    • (2001) Methods Enzymol , vol.339 , pp. 258-270
    • Dyson, H.J.1    Wright, P.E.2
  • 12
    • 16244419001 scopus 로고    scopus 로고
    • Elucidation of the protein folding landscape by NMR
    • Dyson, H. J., and Wright, P. E. (2005) Elucidation of the protein folding landscape by NMR, Methods Enzymol. 394, 299-321.
    • (2005) Methods Enzymol , vol.394 , pp. 299-321
    • Dyson, H.J.1    Wright, P.E.2
  • 13
    • 33846913510 scopus 로고    scopus 로고
    • Atomic-level characterization of disordered protein ensembles
    • Mittag, T., and Forman-Kay, J. D. (2007) Atomic-level characterization of disordered protein ensembles, Curr. Opin. Struct. Biol. 17, 3-14.
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 3-14
    • Mittag, T.1    Forman-Kay, J.D.2
  • 15
    • 34247616119 scopus 로고    scopus 로고
    • Towards proteomic approaches for the identification of structural disorder
    • Csizmok, V., Dosztanyi, Z., Simon, I., and Tompa, P. (2007) Towards proteomic approaches for the identification of structural disorder, Curr. Protein Pept. Sci. 8, 173-179.
    • (2007) Curr. Protein Pept. Sci , vol.8 , pp. 173-179
    • Csizmok, V.1    Dosztanyi, Z.2    Simon, I.3    Tompa, P.4
  • 16
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • Choy, W. Y., and Forman-Kay, J. D. (2001) Calculation of ensembles of structures representing the unfolded state of an SH3 domain, J. Mol. Biol. 308, 1011-1032.
    • (2001) J. Mol. Biol , vol.308 , pp. 1011-1032
    • Choy, W.Y.1    Forman-Kay, J.D.2
  • 17
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter, M., Simon, I., Friedrich, P., and Tompa, P. (2004) Preformed structural elements feature in partner recognition by intrinsically unstructured proteins, J. Mol. Biol. 338, 1015-1026.
    • (2004) J. Mol. Biol , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 19
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa, P., Szasz, C., and Buday, L. (2005) Structural disorder throws new light on moonlighting, Trends Biochem. Sci. 30, 484-489.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 20
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • Fuxreiter, M., Tompa, P., and Simon, I. (2007) Local structural disorder imparts plasticity on linear motifs, Bioinformatics 23, 950-956.
    • (2007) Bioinformatics , vol.23 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 21
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets: The roles of intrinsic disorder in protein interaction networks
    • Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., and Uversky, V. N. (2005) Flexible nets: The roles of intrinsic disorder in protein interaction networks, FEBS J. 272, 5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 22
    • 0036147568 scopus 로고    scopus 로고
    • Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations
    • Ma, B., Shatsky, M., Wolfson, H. J., and Nussinov, R. (2002) Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations, Protein Sci. 11, 184-197.
    • (2002) Protein Sci , vol.11 , pp. 184-197
    • Ma, B.1    Shatsky, M.2    Wolfson, H.J.3    Nussinov, R.4
  • 23
    • 0035014892 scopus 로고    scopus 로고
    • NMR spin relaxation methods for characterization of disorder and folding in proteins
    • Bracken, C. (2001) NMR spin relaxation methods for characterization of disorder and folding in proteins, J. Mol. Graphics Modell. 19, 3-12.
    • (2001) J. Mol. Graphics Modell , vol.19 , pp. 3-12
    • Bracken, C.1
  • 24
    • 0035017534 scopus 로고    scopus 로고
    • NMR and SAXS characterization of the denatured state of the chemotactic protein cheY: Implications for protein folding initiation
    • Garcia, P., Serrano, L., Durand, D., Rico, M., and Bruix, M. (2001) NMR and SAXS characterization of the denatured state of the chemotactic protein cheY: Implications for protein folding initiation, Protein Sci. 10, 1100-1112.
    • (2001) Protein Sci , vol.10 , pp. 1100-1112
    • Garcia, P.1    Serrano, L.2    Durand, D.3    Rico, M.4    Bruix, M.5
  • 25
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson, H. J., and Wright, P. E. (2004) Unfolded proteins and protein folding studied by NMR, Chem. Rev. 104, 3607-3622.
    • (2004) Chem. Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 27
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase, K., Dyson, H. J., and Wright, P. E. (2007) Mechanism of coupled folding and binding of an intrinsically disordered protein, Nature 447, 1021-1025.
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 28
    • 0000095902 scopus 로고
    • Prothymosin a: Isolation and properties of the major immunoreactive form of thymosin α1 in rat thymus
    • Haritos, A. A., Goodall, G. J., and Horecker, B. L. (1984) Prothymosin a: Isolation and properties of the major immunoreactive form of thymosin α1 in rat thymus, Proc. Natl. Acad. Sci. U.S.A. 81, 1008-1011.
    • (1984) Proc. Natl. Acad. Sci. U.S.A , vol.81 , pp. 1008-1011
    • Haritos, A.A.1    Goodall, G.J.2    Horecker, B.L.3
  • 29
    • 0033783289 scopus 로고    scopus 로고
    • Fifteen years of prothymosin α: Contradictory past and new horizons
    • Pineiro, A., Cordero, O. J., and Nogueira, M. (2000) Fifteen years of prothymosin α: Contradictory past and new horizons, Peptides 21, 1433-1446.
    • (2000) Peptides , vol.21 , pp. 1433-1446
    • Pineiro, A.1    Cordero, O.J.2    Nogueira, M.3
  • 31
    • 33645468595 scopus 로고    scopus 로고
    • Surfing on prothymosin α proliferation and anti-apoptotic properties
    • Letsas, K. P., and Frangou-Lazaridis, M. (2006) Surfing on prothymosin α proliferation and anti-apoptotic properties, Neoplasma 53, 92-96.
    • (2006) Neoplasma , vol.53 , pp. 92-96
    • Letsas, K.P.1    Frangou-Lazaridis, M.2
  • 32
    • 0028276120 scopus 로고
    • Prothymosin α binds to histone H1 in vitro
    • Papamarcaki, T., and Tsolas, O. (1994) Prothymosin α binds to histone H1 in vitro, FEBS Lett. 345, 71-75.
    • (1994) FEBS Lett , vol.345 , pp. 71-75
    • Papamarcaki, T.1    Tsolas, O.2
  • 34
    • 0036245548 scopus 로고    scopus 로고
    • Prothymosin α interacts with the CREB-binding protein and potentiates transcription,
    • 3
    • Karetsou, Z., Kretsovali, A., Murphy, C., Tsolas, O., and Papamarcaki, T. (2002) Prothymosin α interacts with the CREB-binding protein and potentiates transcription, EMBO Rep. 3, 361-366.
    • (2002) EMBO Rep , pp. 361-366
    • Karetsou, Z.1    Kretsovali, A.2    Murphy, C.3    Tsolas, O.4    Papamarcaki, T.5
  • 35
  • 38
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • McMahon, M., Itoh, K., Yamamoto, M., and Hayes, J. D. (2003) Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression, J. Biol. Chem. 278, 21592-21600.
    • (2003) J. Biol. Chem , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 39
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein, J. C., Waterhouse, N. J., Juin, P., Evan, G. I., and Green, D. R. (2000) The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant, Nat. Cell Biol. 2, 156-162.
    • (2000) Nat. Cell Biol , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 40
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. (2001) The expanding role of mitochondria in apoptosis, Genes Dev. 15, 2922-2933.
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 41
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • Acehan, D., Jiang, X., Morgan, D. G., Heuser, J. E., Wang, X., and Akey, C. W. (2002) Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation, Mol. Cell 9, 423-432.
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 42
    • 0036899079 scopus 로고    scopus 로고
    • Apoptosomes: Engines for caspase activation
    • Adams, J. M., and Cory, S. (2002) Apoptosomes: Engines for caspase activation, Curr. Opin. Cell Biol. 14, 715-720.
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 715-720
    • Adams, J.M.1    Cory, S.2
  • 43
    • 0034613302 scopus 로고    scopus 로고
    • Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1
    • Jiang, X., and Wang, X. (2000) Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1, J. Biol. Chem. 275, 31199-31203.
    • (2000) J. Biol. Chem , vol.275 , pp. 31199-31203
    • Jiang, X.1    Wang, X.2
  • 44
    • 0036121272 scopus 로고    scopus 로고
    • Apoptosome: The cellular engine for the activation of caspase-9
    • Shi, Y. (2002) Apoptosome: The cellular engine for the activation of caspase-9, Structure 10, 285-288.
    • (2002) Structure , vol.10 , pp. 285-288
    • Shi, Y.1
  • 49
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions
    • Uversky, V. N., Gillespie, J. R., and Fink, A. L. (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions, Proteins 41, 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 52
    • 36048953275 scopus 로고    scopus 로고
    • A new protocol for high-yield purification of recombinant human prothymosin α expressed in Escherichia coli for NMR studies
    • in press
    • Yi, S., Brickenden, A., and Choy, W. Y. (2007) A new protocol for high-yield purification of recombinant human prothymosin α expressed in Escherichia coli for NMR studies, Protein Expression Purif., in press.
    • (2007) Protein Expression Purif
    • Yi, S.1    Brickenden, A.2    Choy, W.Y.3
  • 53
    • 0037465668 scopus 로고    scopus 로고
    • A novel strategy for the purification of recombinantly expressed unstructured protein domains
    • Kalthoff, C. (2003) A novel strategy for the purification of recombinantly expressed unstructured protein domains, J. Chromatogr., B 786, 247-254.
    • (2003) J. Chromatogr., B , vol.786 , pp. 247-254
    • Kalthoff, C.1
  • 55
    • 0029400480 scopus 로고
    • NMRPIPE: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPIPE: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 56
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules, Methods Mol. Biol. 278, 313-352.
    • (2004) Methods Mol. Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 57
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler, M., Schleucher, J., and Griesinger, C. (1999) Heteronuclear multimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients, Prog. Nucl. Magn. Reson. Spectrosc. 34, 93-158.
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 58
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri, A. S., Hinton, D. P., and Byrd, R. A. (1995) Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements, J. Am. Chem. Soc. 117, 7566-7567.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 59
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D. K., Grimshaw, S. B., Receveur, V., Dobson, C. M., Jones, J. A., and Smith, L. J. (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques, Biochemistry 38, 16424-16431.
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 60
    • 0001144784 scopus 로고    scopus 로고
    • 1 constant relaxation time NMRspectroscopy
    • 1 constant relaxation time NMRspectroscopy, J. Am. Chem. Soc. 118, 911-912.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 911-912
    • Akke, M.1    Palmer, A.G.2
  • 62
    • 0028472289 scopus 로고
    • Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods
    • Davis, D. G., Perlman, M. E., and London, R. E. (1994) Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods, J. Magn. Reson., Ser. B 104, 266-275.
    • (1994) J. Magn. Reson., Ser. B , vol.104 , pp. 266-275
    • Davis, D.G.1    Perlman, M.E.2    London, R.E.3
  • 64
    • 0032148390 scopus 로고    scopus 로고
    • A microfabricated dialysis device for sample cleanup in electrospray ionization mass spectrometry
    • Xu, N., Lin, Y., Hofstadler, S. A., Matson, D., Call, C. J., and Smith, R. D. (1998) A microfabricated dialysis device for sample cleanup in electrospray ionization mass spectrometry, Anal. Chem. 70, 3553-3556.
    • (1998) Anal. Chem , vol.70 , pp. 3553-3556
    • Xu, N.1    Lin, Y.2    Hofstadler, S.A.3    Matson, D.4    Call, C.J.5    Smith, R.D.6
  • 65
    • 0036034098 scopus 로고    scopus 로고
    • On-line microdialysis for enhanced resolution and sensitivity during electrospray mass spectrometry of non-covalent complexes and competitive binding studies
    • Benkestock, K., Edlund, P. O., and Roeraade, J. (2002) On-line microdialysis for enhanced resolution and sensitivity during electrospray mass spectrometry of non-covalent complexes and competitive binding studies, Rapid Commun. Mass Spectrom. 16, 2054-2059.
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , pp. 2054-2059
    • Benkestock, K.1    Edlund, P.O.2    Roeraade, J.3
  • 66
    • 0347610773 scopus 로고
    • 13C nulcear magnetic resonance chemical shifts
    • 13C nulcear magnetic resonance chemical shifts, J. Am. Chem. Soc. 113, 5490-5492.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 67
    • 23144462958 scopus 로고    scopus 로고
    • Linear analysis of carbon-13 chemical shift differences and its application to the detection and correction of errors in referencing and spin system identifications
    • Wang, L., Eghbalnia, H. R., Bahrami, A., and Markley, J. L. (2005) Linear analysis of carbon-13 chemical shift differences and its application to the detection and correction of errors in referencing and spin system identifications, J. Biomol. NMR 32, 13-22.
    • (2005) J. Biomol. NMR , vol.32 , pp. 13-22
    • Wang, L.1    Eghbalnia, H.R.2    Bahrami, A.3    Markley, J.L.4
  • 69
    • 0034727681 scopus 로고    scopus 로고
    • Methanol-induced conformations of myoglobin at pH 4.0
    • Babu, K. R., and Douglas, D. J. (2000) Methanol-induced conformations of myoglobin at pH 4.0, Biochemistry 39, 14702-14710.
    • (2000) Biochemistry , vol.39 , pp. 14702-14710
    • Babu, K.R.1    Douglas, D.J.2
  • 71
    • 0030027168 scopus 로고    scopus 로고
    • Analysis of the absorption spectrum of photosystem II reaction centers: Temperature dependence, pigment assignment, and inhomogeneous broadening
    • Konermann, L., and Holzwarth, A. R. (1996) Analysis of the absorption spectrum of photosystem II reaction centers: Temperature dependence, pigment assignment, and inhomogeneous broadening, Biochemistry 35, 829-842.
    • (1996) Biochemistry , vol.35 , pp. 829-842
    • Konermann, L.1    Holzwarth, A.R.2
  • 72
    • 0028390789 scopus 로고
    • Conformation or cytochrome c studied by deuterium exchange-electrospray ionization mass spectrometry
    • Wagner, D. S., and Anderegg, R. J. (1994) Conformation or cytochrome c studied by deuterium exchange-electrospray ionization mass spectrometry, Anal. Chem. 66, 706-711.
    • (1994) Anal. Chem , vol.66 , pp. 706-711
    • Wagner, D.S.1    Anderegg, R.J.2
  • 73
    • 36049023019 scopus 로고    scopus 로고
    • Mass Spectrometry
    • John Wiley and Sons Inc, Hoboken, NJ
    • Kaltashov, I. A., and Eyles, S. J. (2005) Mass Spectrometry, in Biophysics, John Wiley and Sons Inc., Hoboken, NJ.
    • (2005) Biophysics
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 74
    • 34347332295 scopus 로고    scopus 로고
    • A minimalist model for exploring conformational effects on the electrospray charge state distribution of proteins
    • Konermann, L. (2007) A minimalist model for exploring conformational effects on the electrospray charge state distribution of proteins, J. Phys. Chem. B 111, 6534-6543.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 6534-6543
    • Konermann, L.1
  • 75
    • 34250748490 scopus 로고    scopus 로고
    • Analysis of protein mixtures by electrospray mass spectrometry: Effects of conformation and desolvation behavior on the signal intensities of hemoglobin subunits
    • Kuprowski, M. C., Boys, B. L., and Konermann, L. (2007) Analysis of protein mixtures by electrospray mass spectrometry: Effects of conformation and desolvation behavior on the signal intensities of hemoglobin subunits, J. Am. Soc. Mass Spectrom. 18, 1279-1285.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 1279-1285
    • Kuprowski, M.C.1    Boys, B.L.2    Konermann, L.3
  • 76
    • 33947377924 scopus 로고    scopus 로고
    • Signal response of co-existing protein conformers in electrospray mass spectrometry
    • Kuprowski, M. C., and Konermann, L. (2007) Signal response of co-existing protein conformers in electrospray mass spectrometry, Anal. Chem. 79, 2499-2506.
    • (2007) Anal. Chem , vol.79 , pp. 2499-2506
    • Kuprowski, M.C.1    Konermann, L.2
  • 77
    • 0028559743 scopus 로고
    • Calcium stoichiometry determination for calcium binding proteins by electrospray ionization mass spectrometry
    • Hu, P. F., Ye, Q. Z., and Loo, J. A. (1994) Calcium stoichiometry determination for calcium binding proteins by electrospray ionization mass spectrometry, Anal. Chem. 66, 4190-4194.
    • (1994) Anal. Chem , vol.66 , pp. 4190-4194
    • Hu, P.F.1    Ye, Q.Z.2    Loo, J.A.3
  • 78
    • 3242671533 scopus 로고    scopus 로고
    • Buffer loading for counteracting metal salt-induced signal suppression in electrospray ionization
    • Iavarone, A. T., Udekwu, O. A., and Williams, E. R. (2004) Buffer loading for counteracting metal salt-induced signal suppression in electrospray ionization, Anal. Chem. 76, 3944-3950.
    • (2004) Anal. Chem , vol.76 , pp. 3944-3950
    • Iavarone, A.T.1    Udekwu, O.A.2    Williams, E.R.3
  • 79
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 80
    • 0031853060 scopus 로고    scopus 로고
    • Protein dynamics from NMR
    • Kay, L. E. (1998) Protein dynamics from NMR, Nat. Struct. Biol. NMR 513-517.
    • (1998) Nat. Struct. Biol. NMR , pp. 513-517
    • Kay, L.E.1
  • 82
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation- compensated Carr-Purcell-Meiboom-Gill sequence for character-izing chemical exchange by NMR spectroscopy
    • Loria, J. P., Ranee, M., and Palmer, A. G. (1999) A relaxation- compensated Carr-Purcell-Meiboom-Gill sequence for character-izing chemical exchange by NMR spectroscopy, J. Am. Chem. Soc. 121, 2331-2332.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Ranee, M.2    Palmer, A.G.3
  • 83
    • 0027988297 scopus 로고
    • Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease
    • Alexandrescu, A. T., and Shortle, D. (1994) Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease, J. Mol. Biol. 242, 527-546.
    • (1994) J. Mol. Biol , vol.242 , pp. 527-546
    • Alexandrescu, A.T.1    Shortle, D.2
  • 84
    • 0026784152 scopus 로고
    • Mapping of the spectral densities of N-H bond motions in Eglin c using heteronuclear relaxation experiments
    • Peng, J. W., and Wagner, G. (1992) Mapping of the spectral densities of N-H bond motions in Eglin c using heteronuclear relaxation experiments, Biochemistry 31, 8571-8576.
    • (1992) Biochemistry , vol.31 , pp. 8571-8576
    • Peng, J.W.1    Wagner, G.2
  • 86
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins, Curr. Opin. Struct. Biol. 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 87
    • 33344463325 scopus 로고    scopus 로고
    • Keapl recruits Neh2 through binding to ETGE and DLG motifs: Characterization of the two-site molecular recognition model
    • Tong, K. I., Katoh, Y., Kusunoki, H., Itoh, K., Tanaka, T., and Yamamoto, M. (2006) Keapl recruits Neh2 through binding to ETGE and DLG motifs: Characterization of the two-site molecular recognition model, Mol. Cell. Biol. 26, 2887-2900.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2887-2900
    • Tong, K.I.1    Katoh, Y.2    Kusunoki, H.3    Itoh, K.4    Tanaka, T.5    Yamamoto, M.6
  • 88
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: Methods, structures, function, and disease
    • Millhauser, G. L. (2007) Copper and the prion protein: Methods, structures, function, and disease, Annu. Rev. Phys. Chem. 58, 299-320.
    • (2007) Annu. Rev. Phys. Chem , vol.58 , pp. 299-320
    • Millhauser, G.L.1
  • 89
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular link between parkinson's disease and heavy metal exposure
    • Uversky, V. N., Li, J., and Fink, A. L. (2001) Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular link between parkinson's disease and heavy metal exposure, J. Biol. Chem. 276, 44284-44296.
    • (2001) J. Biol. Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 90
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng, R., Jenkins, T. M., and Craigie, R. (1996) Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity, Proc. Natl. Acad. Sci. U.S.A. 93, 13659-13664.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3


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