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Volumn 138, Issue 2, 1999, Pages 244-255

Superslow Backbone Protein Dynamics as Studied by 1D Solid-State MAS Exchange NMR Spectroscopy

Author keywords

Barstar; Exchange NMR; Polyglycine; Protein dynamics; Spin diffusion

Indexed keywords

BACTERIAL PROTEIN; BARSTAR PROTEIN, BACILLUS AMYLOLIQUEFACIENS; CARBON; FREE RADICAL; NITROGEN; PEPTIDE; POLYGLYCINE; WATER;

EID: 0033142909     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1999.1733     Document Type: Article
Times cited : (30)

References (35)
  • 3
    • 0001920774 scopus 로고    scopus 로고
    • Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: Application to ribonuclease T1
    • J. Engelke, and H. Rueterjans, Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: Application to ribonuclease T1, J. Biomol. NMR 9, 63-78 (1997).
    • (1997) J. Biomol. NMR , vol.9 , pp. 63-78
    • Engelke, J.1    Rueterjans, H.2
  • 6
  • 8
    • 0001535072 scopus 로고
    • An NMR study of the backbone dynamics of staphylococcal nuclease in the crystalline state
    • H. B. R. Cole, and D. A. Torchia, An NMR study of the backbone dynamics of staphylococcal nuclease in the crystalline state, Chem. Phys. 158, 271-282 (1991).
    • (1991) Chem. Phys. , vol.158 , pp. 271-282
    • Cole, H.B.R.1    Torchia, D.A.2
  • 10
    • 0030034685 scopus 로고    scopus 로고
    • Dynamics of the three methionyl side chains of Streptomyces subtilisin inhibitor: Deuterium NMR studies in solution and in the solid state
    • A. Tamura, M. Matsushita, A. Naito, S. Kojima, K.-I. Miura, and K. Akasaka, Dynamics of the three methionyl side chains of Streptomyces subtilisin inhibitor: Deuterium NMR studies in solution and in the solid state, Protein Science 5, 127-139 (1996).
    • (1996) Protein Science , vol.5 , pp. 127-139
    • Tamura, A.1    Matsushita, M.2    Naito, A.3    Kojima, S.4    Miura, K.-I.5    Akasaka, K.6
  • 12
    • 0030617281 scopus 로고    scopus 로고
    • 13C-NMR study on the conformational and dynamical properties of a cereal seed storage protein, C-hordein, and its model peptides
    • 13C-NMR study on the conformational and dynamical properties of a cereal seed storage protein, C-hordein, and its model peptides, Biopolymers 41, 289-300 (1997).
    • (1997) Biopolymers , vol.41 , pp. 289-300
    • Gil, A.M.1    Masui, K.2    Naito, A.3    Tatham, A.S.4    Belton, P.S.5    Saito, H.6
  • 14
    • 0031547533 scopus 로고    scopus 로고
    • 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A
    • 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A, J. Mol. Biol. 268, 494-511 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 494-511
    • Wong, K.-B.1    Fersht, A.R.2    Freund, S.M.V.3
  • 16
  • 17
    • 0031984752 scopus 로고    scopus 로고
    • Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain
    • M. Akke, J. Liu, J. Cavanagh, H. P. Erickson, and A. G. Palmer, Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain, Nat. Struct. Biol. 5, 55-59 (1998).
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 55-59
    • Akke, M.1    Liu, J.2    Cavanagh, J.3    Erickson, H.P.4    Palmer, A.G.5
  • 18
    • 0032517325 scopus 로고    scopus 로고
    • 15N transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins: Application to HIV-1 protease
    • 15N transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins: Application to HIV-1 protease, J. Am. Chem. Soc. 120, 10534-10542 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10534-10542
    • Ishima, R.1    Wingfield, P.T.2    Stahl, S.J.3    Kaufmann, J.D.4    Torchia, D.A.5
  • 19
    • 0000924491 scopus 로고    scopus 로고
    • Time-reverse ODESSA. A 1D exchange experiment for rotating solids with several groups of equivalent nuclei
    • D. Reichert, H. Zimmermann, T. P. Tekely, R. Poupko, and Z. Luz, Time-reverse ODESSA. A 1D exchange experiment for rotating solids with several groups of equivalent nuclei, J. Magn. Reson. 125, 245-258 (1997).
    • (1997) J. Magn. Reson. , vol.125 , pp. 245-258
    • Reichert, D.1    Zimmermann, H.2    Tekely, T.P.3    Poupko, R.4    Luz, Z.5
  • 20
    • 0024453699 scopus 로고
    • Barnase and barstar: Two small proteins to fold and fit together
    • R. W. Hartley, Barnase and barstar: two small proteins to fold and fit together, Trends Biochem. Sci. 14, 450-454 (1989).
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 450-454
    • Hartley, R.W.1
  • 21
    • 0027177102 scopus 로고
    • Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
    • G. Schreiber, and A. R. Fersht, Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering, Biochemistry 32, 5145-5150 (1993).
    • (1993) Biochemistry , vol.32 , pp. 5145-5150
    • Schreiber, G.1    Fersht, A.R.2
  • 22
    • 0027424466 scopus 로고
    • Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen-deuterium exchange
    • D. N. M. Jones, M. Bycroft, M. J. Lubienski, and A. R. Fersht, Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen-deuterium exchange, FEBS Lett. 331, 165-172 (1993).
    • (1993) FEBS Lett. , vol.331 , pp. 165-172
    • Jones, D.N.M.1    Bycroft, M.2    Lubienski, M.J.3    Fersht, A.R.4
  • 24
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • F. M. Studier, and B. A. Moffatt, Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes, J. Mol. Biol. 189, 113-130 (1986).
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.M.1    Moffatt, B.A.2
  • 28
    • 85005481081 scopus 로고
    • Rotor synchronized MAS two-dimensional exchange NMR in solids. Principles and applications
    • Z. Luz, H. W. Spiess, and J. J. Titman, Rotor synchronized MAS two-dimensional exchange NMR in solids. Principles and applications, Isr. J. Chem. 32, 145-160 (1992).
    • (1992) Isr. J. Chem. , vol.32 , pp. 145-160
    • Luz, Z.1    Spiess, H.W.2    Titman, J.J.3
  • 29
    • 49349127089 scopus 로고
    • 1 values by a method which suppresses artifacts
    • 1 values by a method which suppresses artifacts, J. Magn. Reson 30, 613-616 (1978).
    • (1978) J. Magn. Reson , vol.30 , pp. 613-616
    • Torchia, D.A.1
  • 31
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules
    • G. Lipari and A. Szabo, Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules, J. Amer. Chem. Soc. 104, 4546-4559 (1982).
    • (1982) J. Amer. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 32
    • 0002933224 scopus 로고    scopus 로고
    • Carbon-13 chemical-shift correlation, spin diffusion and self diffusion in isotopically enriched tropolone
    • Z. Olender, D. Reichert, A. Muller, H. Zimmermann, R. Poupko, and Z. Luz, Carbon-13 chemical-shift correlation, spin diffusion and self diffusion in isotopically enriched tropolone, J. Magn. Reson. A120, 31-45 (1996).
    • (1996) J. Magn. Reson. , vol.A120 , pp. 31-45
    • Olender, Z.1    Reichert, D.2    Muller, A.3    Zimmermann, H.4    Poupko, R.5    Luz, Z.6
  • 34
    • 33750405141 scopus 로고
    • Sideband intensities in NMR spectra of samples spinning at the magic angle
    • J. Herzfeld and A. Berger, Sideband intensities in NMR spectra of samples spinning at the magic angle, J. Chem. Phys. 73, 6021-6030 (1980).
    • (1980) J. Chem. Phys. , vol.73 , pp. 6021-6030
    • Herzfeld, J.1    Berger, A.2


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