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Volumn 36, Issue 11, 2003, Pages 858-865

High-Resolution Solid-State NMR Applied to Polypeptides and Membrane Proteins

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; POLYPEPTIDE;

EID: 0344393786     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar020232y     Document Type: Review
Times cited : (93)

References (50)
  • 1
    • 0034764117 scopus 로고    scopus 로고
    • The way to NMR structures of proteins
    • Wüthrich, K. The way to NMR structures of proteins. Nat. Struct. Biol. 2001, 8, 923-925.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 923-925
    • Wüthrich, K.1
  • 2
    • 0036841958 scopus 로고    scopus 로고
    • Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions
    • Horwich, A. Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions. J. Clin. Invest. 2002, 110, 1221-1232.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1221-1232
    • Horwich, A.1
  • 3
    • 33745315198 scopus 로고
    • Nuclear magnetic resonance spectra from a crystal rotated at high speed
    • Andrew, E. R.; Bradbury, A.; Eades, R. G. Nuclear magnetic resonance spectra from a crystal rotated at high speed. Nature 1958, 182, 1659.
    • (1958) Nature , vol.182 , pp. 1659
    • Andrew, E.R.1    Bradbury, A.2    Eades, R.G.3
  • 5
    • 33646720540 scopus 로고    scopus 로고
    • Total correlation spectroscopy in the solid state. The use of scalar couplings to determine the through-bond connectivity
    • Baldus, M.; Meier, B. H. Total correlation spectroscopy in the solid state. The use of scalar couplings to determine the through-bond connectivity. J. Magn. Reson. Ser. A 1996, 121, 65-69.
    • (1996) J. Magn. Reson. Ser. A , vol.121 , pp. 65-69
    • Baldus, M.1    Meier, B.H.2
  • 6
    • 0031853671 scopus 로고    scopus 로고
    • Dipolar recoupling in MAS spectra of biological solids
    • Griffin, R. G. Dipolar recoupling in MAS spectra of biological solids. Nat. Struct. Biol. 1998, 5, 508-512.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 508-512
    • Griffin, R.G.1
  • 7
    • 0037008857 scopus 로고    scopus 로고
    • Correlation experiments for assignment and structure elucidation of immobilized polypeptides under magic angle spinning
    • Baldus, M. Correlation experiments for assignment and structure elucidation of immobilized polypeptides under magic angle spinning. Prog. Nucl. Magn. Reson. Spectrosc. 2002, 41, 1-47.
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc. , vol.41 , pp. 1-47
    • Baldus, M.1
  • 8
    • 0002084353 scopus 로고    scopus 로고
    • Adiabatic homonuclear polarization transfer in magic angle spinning solid-state NMR
    • Verel, R.; Baldus, M.; Nijman, M.; van Os, J. W. M.; Meier, B. H. Adiabatic homonuclear polarization transfer in magic angle spinning solid-state NMR. Chem. Phys. Lett. 1997, 280, 31-39.
    • (1997) Chem. Phys. Lett. , vol.280 , pp. 31-39
    • Verel, R.1    Baldus, M.2    Nijman, M.3    Van Os, J.W.M.4    Meier, B.H.5
  • 9
    • 0000368822 scopus 로고    scopus 로고
    • Cross polarization in the tilted frame: Assignment and spectral simplification in heteronuclear spin systems
    • Baldus, M.; Petkova, A. T.; Herzfeld, J.; Griffin, R. G. Cross polarization in the tilted frame: Assignment and spectral simplification in heteronuclear spin systems. Mol. Phys. 1998, 95, 1197-1207.
    • (1998) Mol. Phys. , vol.95 , pp. 1197-1207
    • Baldus, M.1    Petkova, A.T.2    Herzfeld, J.3    Griffin, R.G.4
  • 10
    • 0037151636 scopus 로고    scopus 로고
    • Structural constraints from proton-mediated rare-spin correlation spectroscopy in rotating solids
    • Lange, A.; Luca, S.; Baldus, M. Structural constraints from proton-mediated rare-spin correlation spectroscopy in rotating solids. J. Am. Chem. Soc. 2002, 124, 9704-9705.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9704-9705
    • Lange, A.1    Luca, S.2    Baldus, M.3
  • 12
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 1991, 113, 5490-5492.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 13
    • 0027308278 scopus 로고
    • Secondary and tertiary structural effects on protein NMR chemical shifts - An ab initio approach
    • Dedios, A. C.; Pearson, J. G.; Oldfield, E. Secondary and tertiary structural effects on protein NMR chemical shifts - an ab initio approach. Science 1993, 260, 1491-1496.
    • (1993) Science , vol.260 , pp. 1491-1496
    • Dedios, A.C.1    Pearson, J.G.2    Oldfield, E.3
  • 14
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by A beta(16-22), a seven-residue fragment of the Alzheimer's betaamyloid peptide, and structural characterization by solid state NMR
    • Balbach, J. J.; Ishii, Y.; Antzutkin, O. N.; Leapman, R. D.; Rizzo, N. W.; Dyda, F.; Reed, J.; Tycko, R. Amyloid fibril formation by A beta(16-22), a seven-residue fragment of the Alzheimer's betaamyloid peptide, and structural characterization by solid state NMR. Biochemistry 2000, 39, 13748-13759.
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzutkin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5    Dyda, F.6    Reed, J.7    Tycko, R.8
  • 15
    • 0034846331 scopus 로고    scopus 로고
    • Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under magic angle spinning
    • Luca, S.; Filippov, D. V.; van Boom, J. H.; Oschkinat, H.; de Groot, H. J. M.; Baldus, M. Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under magic angle spinning. J. Biomol. NMR 2001, 20, 325-331.
    • (2001) J. Biomol. NMR , vol.20 , pp. 325-331
    • Luca, S.1    Filippov, D.V.2    Van Boom, J.H.3    Oschkinat, H.4    De Groot, H.J.M.5    Baldus, M.6
  • 16
    • 0035544152 scopus 로고    scopus 로고
    • 13C′ chemical shifts in proteins using a density functional database
    • 13C′ chemical shifts in proteins using a density functional database. J. Biomol. NMR 2001, 21, 321-333.
    • (2001) J. Biomol. NMR , vol.21 , pp. 321-333
    • Xu, X.P.1    Case, D.A.2
  • 17
    • 0036923765 scopus 로고    scopus 로고
    • Enhanced spectral resolution in immobilized peptides and proteins by combining chemical shift sum and difference spectroscopy
    • Luca, S.; Baldus, M. Enhanced spectral resolution in immobilized peptides and proteins by combining chemical shift sum and difference spectroscopy. J. Magn. Reson. 2002, 159, 243-249.
    • (2002) J. Magn. Reson. , vol.159 , pp. 243-249
    • Luca, S.1    Baldus, M.2
  • 18
    • 0141988942 scopus 로고    scopus 로고
    • Analysis of proton-proton transfer dynamics in rotating solids and their use for 3D structure determination
    • in press
    • Lange, A.; Seidel, K.; Verdier, L.; Luca, S.; Baldus, M. Analysis of proton-proton transfer dynamics in rotating solids and their use for 3D structure determination. J. Am. Chem. Soc. 2003, in press.
    • (2003) J. Am. Chem. Soc.
    • Lange, A.1    Seidel, K.2    Verdier, L.3    Luca, S.4    Baldus, M.5
  • 21
    • 0031189051 scopus 로고    scopus 로고
    • Site-resolved determination of peptide torsion angle φ from the relative orientations of backbone N-H and C-H bonds by solid-state NMR
    • Hong, M.; Gross, J. D.; Griffin, R. G. Site-resolved determination of peptide torsion angle φ from the relative orientations of backbone N-H and C-H bonds by solid-state NMR. J. Phys. Chem. B 1997, 101, 5869-5874.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 5869-5874
    • Hong, M.1    Gross, J.D.2    Griffin, R.G.3
  • 22
    • 0002084355 scopus 로고    scopus 로고
    • Solid-state NMR measurement of ψ in peptides: A NCCN 2Q-heteronuclear local field experiment
    • Costa, P. R.; Gross, J. D.; Hong, M.; Griffin, R. G. Solid-state NMR measurement of ψ in peptides: a NCCN 2Q-heteronuclear local field experiment. Chem. Phys. Lett. 1997, 280, 95-103.
    • (1997) Chem. Phys. Lett. , vol.280 , pp. 95-103
    • Costa, P.R.1    Gross, J.D.2    Hong, M.3    Griffin, R.G.4
  • 24
    • 57249096266 scopus 로고    scopus 로고
    • 13C chemical shift anisotropy measurements
    • 13C chemical shift anisotropy measurements. J. Magn. Reson. 2001, 149, 131-138.
    • (2001) J. Magn. Reson. , vol.149 , pp. 131-138
    • Blanco, F.J.1    Tycko, R.2
  • 26
    • 0000345717 scopus 로고
    • Rotational resonance in the tilted rotating frame
    • Takegoshi, K.; Nomura, K.; Terao, T. Rotational resonance in the tilted rotating frame. Chem. Phys. Lett. 1995, 232, 424-428.
    • (1995) Chem. Phys. Lett. , vol.232 , pp. 424-428
    • Takegoshi, K.1    Nomura, K.2    Terao, T.3
  • 29
    • 0031595590 scopus 로고    scopus 로고
    • 15N multidimensional NMR to study the structure and dynamics of proteins
    • 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct. 1998, 27, 357-406.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 31
    • 0033121307 scopus 로고    scopus 로고
    • 13C-labeling of a membrane protein for solid-state NMR investigations
    • 13C-labeling of a membrane protein for solid-state NMR investigations. J. Biomol. NMR 1999, 14, 71-74.
    • (1999) J. Biomol. NMR , vol.14 , pp. 71-74
    • Hong, M.1    Jakes, K.2
  • 33
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic angle spinning NMR spectroscopy
    • Castellani, F.; van Rossum, B.; Diehl, A.; Schubert, M.; Rehbein, K.; Oschkinat, H. Structure of a protein determined by solid-state magic angle spinning NMR spectroscopy. Nature 2002, 420, 98-102.
    • (2002) Nature , vol.420 , pp. 98-102
    • Castellani, F.1    Van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschkinat, H.6
  • 34
    • 0036816798 scopus 로고    scopus 로고
    • Solid-state NMR studies of the structure and mechanisms of proteins
    • Thompson, L. K. Solid-state NMR studies of the structure and mechanisms of proteins. Curr. Opin. Struct. Biol. 2002, 12, 661-669.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 661-669
    • Thompson, L.K.1
  • 35
    • 0035795429 scopus 로고    scopus 로고
    • 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 tesla
    • 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 tesla. Chembiochem 2001, 2, 272-281.
    • (2001) Chembiochem , vol.2 , pp. 272-281
    • Pauli, J.1    Baldus, M.2    Van Rossum, B.3    De Groot, H.4    Oschkinat, H.5
  • 37
    • 0032590227 scopus 로고    scopus 로고
    • 15N-labeled solid proteins by two- and three-dimensional magic angle spinning NMR
    • 15N-labeled solid proteins by two- and three-dimensional magic angle spinning NMR. J. Biomol. NMR 1999, 15, 1-14.
    • (1999) J. Biomol. NMR , vol.15 , pp. 1-14
    • Hong, M.1
  • 40
    • 4244050504 scopus 로고    scopus 로고
    • Solid-state NMR sequential resonance assignments and conformational analysis of the 2*10.4 kDa dimeric form of the bacillus subtilis protein Crh
    • in press
    • Böckmann, A.; Lange, A.; Galinier, A.; Luca, S.; Giraud, N.; Heise, H.; Juy, M.; Montserret, R.; Penin, F.; Baldus, M. Solid-state NMR sequential resonance assignments and conformational analysis of the 2*10.4 kDa dimeric form of the bacillus subtilis protein Crh. J. Biomol. NMR 2003, in press.
    • (2003) J. Biomol. NMR
    • Böckmann, A.1    Lange, A.2    Galinier, A.3    Luca, S.4    Giraud, N.5    Heise, H.6    Juy, M.7    Montserret, R.8    Penin, F.9    Baldus, M.10
  • 41
    • 0033611960 scopus 로고    scopus 로고
    • Determination of the complete structure of a uniformly labeled molecule by rotational resonance solid-state NMR in the tilted rotating frame
    • Nomura, K.; Takegoshi, K.; Terao, T.; Uchida, K.; Kainosho, M. Determination of the complete structure of a uniformly labeled molecule by rotational resonance solid-state NMR in the tilted rotating frame. J. Am. Chem. Soc. 1999, 121, 4064-4065.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4064-4065
    • Nomura, K.1    Takegoshi, K.2    Terao, T.3    Uchida, K.4    Kainosho, M.5
  • 46
    • 0038412551 scopus 로고    scopus 로고
    • Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state
    • Petkova, A. T.; Baldus, M.; Belenky, M.; Hong, M.; Griffin, R. G.; Herzfeld, J. Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state. J. Magn. Reson. 2003, 160, 1-12.
    • (2003) J. Magn. Reson. , vol.160 , pp. 1-12
    • Petkova, A.T.1    Baldus, M.2    Belenky, M.3    Hong, M.4    Griffin, R.G.5    Herzfeld, J.6


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