메뉴 건너뛰기




Volumn 166, Issue 1, 2004, Pages 100-110

Multiple-spin analysis of chemical-shift-selective (13C, 13C) transfer in uniformly labeled biomolecules

Author keywords

Distances; MAS; Polypeptides; Solid state; Structure determination

Indexed keywords

CORRELATION METHODS; ELECTROMAGNETIC WAVE POLARIZATION; NUCLEAR MAGNETIC RESONANCE; PROTEINS; QUANTUM THEORY;

EID: 0346331287     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmr.2003.10.014     Document Type: Article
Times cited : (25)

References (75)
  • 2
    • 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. 182:1958;1659.
    • (1958) Nature , vol.182 , pp. 1659
    • Andrew, E.R.1    Bradbury, A.2    Eades, R.G.3
  • 3
    • 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. 5:1998;508-512.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 508-512
    • Griffin, R.G.1
  • 4
    • 0009580266 scopus 로고    scopus 로고
    • Dipolar recoupling under magic-angle spinning conditions
    • Dusold S., Sebald A. Dipolar recoupling under magic-angle spinning conditions. Annu. Rep. NMR Spectrosc. 41:2000;185-264.
    • (2000) Annu. Rep. NMR Spectrosc. , vol.41 , pp. 185-264
    • Dusold, S.1    Sebald, A.2
  • 5
    • 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. 41:2002;1-47.
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc. , vol.41 , pp. 1-47
    • Baldus, M.1
  • 7
    • 0030437935 scopus 로고    scopus 로고
    • Magic angle spinning NMR spectroscopy of membrane proteins
    • Smith S.O., Aschheim K., Groesbeek M. Magic angle spinning NMR spectroscopy of membrane proteins. Q. Rev. Biophys. 29:1996;395-449.
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 395-449
    • Smith, S.O.1    Aschheim, K.2    Groesbeek, M.3
  • 8
    • 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. 12:2002;661-669.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 661-669
    • Thompson, L.K.1
  • 9
  • 12
    • 0000253545 scopus 로고
    • Rotor-driven spin diffusion in natural-abundance C-13 spin systems
    • Colombo M.G., Meier B.H., Ernst R.R. Rotor-driven spin diffusion in natural-abundance C-13 spin systems. Chem. Phys. Lett. 146:1988;189-196.
    • (1988) Chem. Phys. Lett. , vol.146 , pp. 189-196
    • Colombo, M.G.1    Meier, B.H.2    Ernst, R.R.3
  • 13
    • 36549091040 scopus 로고
    • Theory and simulations of homonuclear spin pair systems in rotating solids
    • Levitt M.H., Raleigh D.P., Creuzet F., Griffin R.G. Theory and simulations of homonuclear spin pair systems in rotating solids. J. Chem. Phys. 92:1990;6347-6364.
    • (1990) J. Chem. Phys. , vol.92 , pp. 6347-6364
    • Levitt, M.H.1    Raleigh, D.P.2    Creuzet, F.3    Griffin, R.G.4
  • 15
    • 0000528084 scopus 로고
    • Analysis of rotational resonance magnetization exchange curves from crystalline peptides
    • Peersen O.B., Groesbeek M., Aimoto S., Smith S.O. Analysis of rotational resonance magnetization exchange curves from crystalline peptides. J. Am. Chem. Soc. 117:1995;7228-7237.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7228-7237
    • Peersen, O.B.1    Groesbeek, M.2    Aimoto, S.3    Smith, S.O.4
  • 17
    • 0030830624 scopus 로고    scopus 로고
    • Rotational resonance tickling: Accurate internuclear distance measurement in solids
    • Costa P.R., Sun B.Q., Griffin R.G. Rotational resonance tickling: accurate internuclear distance measurement in solids. J. Am. Chem. Soc. 119:1997;10821-10830.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10821-10830
    • Costa, P.R.1    Sun, B.Q.2    Griffin, R.G.3
  • 18
    • 0001118886 scopus 로고    scopus 로고
    • Longitudinal rotational resonance echoes in solid state nuclear magnetic resonance: Investigation of zero quantum spin dynamics
    • Karlsson T., Levitt M.H. Longitudinal rotational resonance echoes in solid state nuclear magnetic resonance: investigation of zero quantum spin dynamics. J. Chem. Phys. 109:1998;5493-5507.
    • (1998) J. Chem. Phys. , vol.109 , pp. 5493-5507
    • Karlsson, T.1    Levitt, M.H.2
  • 19
    • 0037420373 scopus 로고    scopus 로고
    • Determination of internuclear distances in uniformly labeled molecules by rotational-resonance solid-state NMR
    • Williamson P.T.F., Verhoeven A., Ernst M., Meier B.H. Determination of internuclear distances in uniformly labeled molecules by rotational-resonance solid-state NMR. J. Am. Chem. Soc. 125:2003;2718-2722.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2718-2722
    • Williamson, P.T.F.1    Verhoeven, A.2    Ernst, M.3    Meier, B.H.4
  • 20
    • 0041467239 scopus 로고    scopus 로고
    • Rotational resonance NMR: Separation of dipolar coupling and zero quantum relaxation
    • Costa P.R., Sun B.Q., Griffin R.G. Rotational resonance NMR: separation of dipolar coupling and zero quantum relaxation. J. Magn. Reson. 164:2003;92-103.
    • (2003) J. Magn. Reson. , vol.164 , pp. 92-103
    • Costa, P.R.1    Sun, B.Q.2    Griffin, R.G.3
  • 21
    • 0001167666 scopus 로고    scopus 로고
    • Spinning-frequency-dependent narrowband RF-driven dipolar recoupling
    • Goobes G., Boender G.J., Vega S. Spinning-frequency-dependent narrowband RF-driven dipolar recoupling. J. Magn. Reson. 146:2000;204-219.
    • (2000) J. Magn. Reson. , vol.146 , pp. 204-219
    • Goobes, G.1    Boender, G.J.2    Vega, S.3
  • 22
    • 0036299470 scopus 로고    scopus 로고
    • Improved narrowband dipolar recoupling for homonuclear distance measurements in rotating solids
    • Goobes G., Vega S. Improved narrowband dipolar recoupling for homonuclear distance measurements in rotating solids. J. Magn. Reson. 154:2002;236-251.
    • (2002) J. Magn. Reson. , vol.154 , pp. 236-251
    • Goobes, G.1    Vega, S.2
  • 23
    • 0037048587 scopus 로고    scopus 로고
    • Determination of multiple torsion-angle constraints in U-C-13,N-15-labeled peptides: 3D H-1-N-15-C-13-H-1 dipolar chemical shift NMR spectroscopy in rotating solids
    • Rienstra C.M., Hohwy M., Mueller L.J., Jaroniec C.P., Reif B., Griffin R.G. Determination of multiple torsion-angle constraints in U-C-13,N-15-labeled peptides: 3D H-1-N-15-C-13-H-1 dipolar chemical shift NMR spectroscopy in rotating solids. J. Am. Chem. Soc. 124:2002;11908-11922.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11908-11922
    • Rienstra, C.M.1    Hohwy, M.2    Mueller, L.J.3    Jaroniec, C.P.4    Reif, B.5    Griffin, R.G.6
  • 24
    • 0032113517 scopus 로고    scopus 로고
    • Experiments and strategies for the assignment of fully C-13/N- 15-labelled polypeptides by solid state NMR
    • Straus S.K., Bremi T., Ernst R.R. Experiments and strategies for the assignment of fully C-13/N- 15-labelled polypeptides by solid state NMR. J. Biomol. NMR. 12:1998;39-50.
    • (1998) J. Biomol. NMR , vol.12 , pp. 39-50
    • Straus, S.K.1    Bremi, T.2    Ernst, R.R.3
  • 25
    • 0032590227 scopus 로고    scopus 로고
    • Resonance assignment of C-13/N-15 labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR
    • Hong M. Resonance assignment of C-13/N-15 labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR. J. Biomol. NMR. 15:1999;1-14.
    • (1999) J. Biomol. NMR , vol.15 , pp. 1-14
    • Hong, M.1
  • 27
    • 0035795429 scopus 로고    scopus 로고
    • Backbone and side-chain C-13 and N-15 signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 tesla
    • Pauli J., Baldus M., van Rossum B., de Groot H., Oschkinat H. Backbone and side-chain C-13 and N-15 signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 tesla. Chembiochem. 2:2001;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
  • 28
    • 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
    • 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. 27:2003;323-339.
    • (2003) J. Biomol. NMR , vol.27 , pp. 323-339
    • 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
  • 30
    • 0037047148 scopus 로고    scopus 로고
    • H-1 and C-13 MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin
    • Creemers A.F.L., Kiihne S., Bovee-Geurts P.H.M., DeGrip W.J., Lugtenburg J., de Groot H.J.M. H-1 and C-13 MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin. Proc. Natl. Acad. Sci. USA. 99:2002;9101-9106.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9101-9106
    • Creemers, A.F.L.1    Kiihne, S.2    Bovee-Geurts, P.H.M.3    Degrip, W.J.4    Lugtenburg, J.5    De Groot, H.J.M.6
  • 31
    • 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. 160:2003;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
  • 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. 420:2002;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
    • 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. 121:1999;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
  • 35
    • 0033939451 scopus 로고    scopus 로고
    • Three-dimensional structure determination of a uniformly labeled molecule by frequency-selective dipolar recoupling under magic-angle spinning
    • Nomura K., Takegoshi K., Terao T., Uchida K., Kainosho M. Three-dimensional structure determination of a uniformly labeled molecule by frequency-selective dipolar recoupling under magic-angle spinning. J. Biomol. NMR. 17:2000;111-123.
    • (2000) J. Biomol. NMR , vol.17 , pp. 111-123
    • Nomura, K.1    Takegoshi, K.2    Terao, T.3    Uchida, K.4    Kainosho, M.5
  • 37
    • 0002996904 scopus 로고    scopus 로고
    • Selectivity of double-quantum-filtered rotational-resonance experiments in larger-than-two-spin systems
    • S. Kiihne, de GrootH.J.M. Dordrecht: Kluwer Academic Publishers
    • Bechmann M., Helluy X., Sebald A. Selectivity of double-quantum-filtered rotational-resonance experiments in larger-than-two-spin systems. Kiihne S., de Groot H.J.M. Focus on Structural Biology. vol. 1:2001;23-31 Kluwer Academic Publishers, Dordrecht.
    • (2001) Focus on Structural Biology , vol.1 , pp. 23-31
    • Bechmann, M.1    Helluy, X.2    Sebald, A.3
  • 38
    • 0037461028 scopus 로고    scopus 로고
    • Multiple-spin effects in fast magic angle spinning Lee-Goldburg cross-polarization experiments in uniformly labeled compounds
    • Ladizhansky V., Vinogradov E., van Rossum B.J., de Groot H.J.M., Vega S. Multiple-spin effects in fast magic angle spinning Lee-Goldburg cross-polarization experiments in uniformly labeled compounds. J. Chem. Phys. 118:2003;5547-5557.
    • (2003) J. Chem. Phys. , vol.118 , pp. 5547-5557
    • Ladizhansky, V.1    Vinogradov, E.2    Van Rossum, B.J.3    De Groot, H.J.M.4    Vega, S.5
  • 39
    • 36149026370 scopus 로고
    • Nuclear double resonance in rotating frame
    • Hartmann S.R., Hahn E.L. Nuclear double resonance in rotating frame. Phys. Rev. 128:1962;2042-2053.
    • (1962) Phys. Rev. , vol.128 , pp. 2042-2053
    • Hartmann, S.R.1    Hahn, E.L.2
  • 40
    • 36849106840 scopus 로고
    • Proton-enhanced NMR of dilute spins in solids
    • Pines A., Gibby M.G., Waugh J.S. Proton-enhanced NMR of dilute spins in solids. J. Chem. Phys. 59:1973;569-590.
    • (1973) J. Chem. Phys. , vol.59 , pp. 569-590
    • Pines, A.1    Gibby, M.G.2    Waugh, J.S.3
  • 41
    • 0001876029 scopus 로고
    • Computer-simulations in magnetic-resonance - An object-oriented programming approach
    • Smith S.A., Levante T.O., Meier B.H., Ernst R.R. Computer-simulations in magnetic-resonance - an object-oriented programming approach. J. Magn. Reson. Ser. A. 106:1994;75-105.
    • (1994) J. Magn. Reson. Ser. A , vol.106 , pp. 75-105
    • Smith, S.A.1    Levante, T.O.2    Meier, B.H.3    Ernst, R.R.4
  • 42
    • 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. 232:1995;424-428.
    • (1995) Chem. Phys. Lett. , vol.232 , pp. 424-428
    • Takegoshi, K.1    Nomura, K.2    Terao, T.3
  • 43
    • 0031201794 scopus 로고    scopus 로고
    • Selective homonuclear polarization transfer in the tilted rotating frame under magic angle spinning in solids
    • Takegoshi K., Nomura K., Terao T. Selective homonuclear polarization transfer in the tilted rotating frame under magic angle spinning in solids. J. Magn. Reson. 127:1997;206-216.
    • (1997) J. Magn. Reson. , vol.127 , pp. 206-216
    • Takegoshi, K.1    Nomura, K.2    Terao, T.3
  • 45
    • 0033170481 scopus 로고    scopus 로고
    • Practical methods for solid-state NMR distance measurements on large biomolecules: Constant-time rotational resonance
    • Balazs Y.S., Thompson L.K. Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance. J. Magn. Reson. 139:1999;371-376.
    • (1999) J. Magn. Reson. , vol.139 , pp. 371-376
    • Balazs, Y.S.1    Thompson, L.K.2
  • 46
    • 43949161069 scopus 로고
    • Ramped-amplitude cross-polarization in magic-angle-spinning NMR
    • Metz G., Wu X.L., Smith S.O. Ramped-amplitude cross-polarization in magic-angle-spinning NMR. J. Magn. Reson. Ser. A. 110:1994;219-227.
    • (1994) J. Magn. Reson. Ser. A , vol.110 , pp. 219-227
    • Metz, G.1    Wu, X.L.2    Smith, S.O.3
  • 47
    • 0034890690 scopus 로고    scopus 로고
    • Methods for sequential resonance assignment in solid, uniformly C-13, N-15 labelled peptides: Quantification and application to antamanide
    • Detken A., Hardy E.H., Ernst M., Kainosho M., Kawakami T., Aimoto S., Meier B.H. Methods for sequential resonance assignment in solid, uniformly C-13, N-15 labelled peptides: quantification and application to antamanide. J. Biomol. NMR. 20:2001;203-221.
    • (2001) J. Biomol. NMR , vol.20 , pp. 203-221
    • Detken, A.1    Hardy, E.H.2    Ernst, M.3    Kainosho, M.4    Kawakami, T.5    Aimoto, S.6    Meier, B.H.7
  • 48
  • 49
    • 36449005555 scopus 로고
    • The Floquet theory of nuclear-magnetic-resonance spectroscopy of single spins and dipolar coupled spin pairs in rotating solids
    • Schmidt A., Vega S. The Floquet theory of nuclear-magnetic-resonance spectroscopy of single spins and dipolar coupled spin pairs in rotating solids. J. Chem. Phys. 96:1992;2655-2680.
    • (1992) J. Chem. Phys. , vol.96 , pp. 2655-2680
    • Schmidt, A.1    Vega, S.2
  • 50
    • 84943491249 scopus 로고
    • Numerical-simulation of magnetic-resonance experiments - Concepts and applications to static, rotating and double rotating experiments
    • Baldus M., Levante T.O., Meier B.H. Numerical-simulation of magnetic-resonance experiments - concepts and applications to static, rotating and double rotating experiments. Z. Naturfors. A. 49:1994;80-88.
    • (1994) Z. Naturfors. A , vol.49 , pp. 80-88
    • Baldus, M.1    Levante, T.O.2    Meier, B.H.3
  • 51
    • 0001734182 scopus 로고
    • Formalized quantum-mechanical floquet theory and its application to sample-spinning in nuclear-magnetic-resonance
    • Levante T.O., Baldus M., Meier B.H., Ernst R.R. Formalized quantum-mechanical floquet theory and its application to sample-spinning in nuclear-magnetic-resonance. Mol. Phys. 86:1995;1195-1212.
    • (1995) Mol. Phys. , vol.86 , pp. 1195-1212
    • Levante, T.O.1    Baldus, M.2    Meier, B.H.3    Ernst, R.R.4
  • 52
    • 0028139553 scopus 로고
    • A method for dihedral angle measurement in solids - Rotational resonance NMR of a transition-state inhibitor of triose phosphate isomerase
    • Tomita Y., Oconnor E.J., McDermott A. A method for dihedral angle measurement in solids - rotational resonance NMR of a transition-state inhibitor of triose phosphate isomerase. J. Am. Chem. Soc. 116:1994;8766-8771.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8766-8771
    • Tomita, Y.1    Oconnor, E.J.2    Mcdermott, A.3
  • 53
    • 0141997193 scopus 로고
    • Photographic neutron-diffraction study of L-histidine Hclh2o by modified Laue method
    • Hohlwein D. Photographic neutron-diffraction study of L-histidine Hclh2o by modified Laue method. Acta Crystallogr. Sect. A. 33:1977;649-654.
    • (1977) Acta Crystallogr. Sect. A , vol.33 , pp. 649-654
    • Hohlwein, D.1
  • 54
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • Vijaykumar S., Bugg C.E., Cook W.J. Structure of ubiquitin refined at 1.8. Å resolution J. Mol. Biol. 194:1987;531-544.
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijaykumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 56
    • 0009580882 scopus 로고
    • Investigations of a nonrandom numerical-method for multidimensional integration
    • Cheng V.B., Suzukawa H.H., Wolfsberg M. Investigations of a nonrandom numerical-method for multidimensional integration. J. Chem. Phys. 59:1973;3992-3999.
    • (1973) J. Chem. Phys. , vol.59 , pp. 3992-3999
    • Cheng, V.B.1    Suzukawa, H.H.2    Wolfsberg, M.3
  • 57
    • 0000325957 scopus 로고    scopus 로고
    • Broadband polarization transfer under magic-angle spinning: Application to total through-space-correlation NMR spectroscopy
    • Baldus M., Meier B.H. Broadband polarization transfer under magic-angle spinning: application to total through-space-correlation NMR spectroscopy. J. Magn. Reson. 128:1997;172-193.
    • (1997) J. Magn. Reson. , vol.128 , pp. 172-193
    • Baldus, M.1    Meier, B.H.2
  • 59
    • 0000369374 scopus 로고    scopus 로고
    • Distance measurements in multiply labeled crystalline cytidines by dipolar recoupling solid state NMR
    • Kiihne S.R., Geahigan K.B., Oyler N.A., Zebroski H., Mehta M.A., Drobny G.P. Distance measurements in multiply labeled crystalline cytidines by dipolar recoupling solid state NMR. J. Phys. Chem. A. 103:1999;3890-3903.
    • (1999) J. Phys. Chem. A , vol.103 , pp. 3890-3903
    • Kiihne, S.R.1    Geahigan, K.B.2    Oyler, N.A.3    Zebroski, H.4    Mehta, M.A.5    Drobny, G.P.6
  • 60
    • 0000432697 scopus 로고    scopus 로고
    • Fivefold symmetric homonuclear dipolar recoupling in rotating solids: Application to double quantum spectroscopy
    • Hohwy M., Rienstra C.M., Jaroniec C.P., Griffin R.G. Fivefold symmetric homonuclear dipolar recoupling in rotating solids: application to double quantum spectroscopy. J. Chem. Phys. 110:1999;7983-7992.
    • (1999) J. Chem. Phys. , vol.110 , pp. 7983-7992
    • Hohwy, M.1    Rienstra, C.M.2    Jaroniec, C.P.3    Griffin, R.G.4
  • 61
    • 0033155783 scopus 로고    scopus 로고
    • The accuracy of distance measurements in solid-state NMR
    • Hodgkinson P., Emsley L. The accuracy of distance measurements in solid-state NMR. J. Magn. Reson. 139:1999;46-59.
    • (1999) J. Magn. Reson. , vol.139 , pp. 46-59
    • Hodgkinson, P.1    Emsley, L.2
  • 62
    • 0001222666 scopus 로고    scopus 로고
    • Polarization transfer dynamics in Lee-Goldburg cross polarization nuclear magnetic resonance experiments on rotating solids
    • Ladizhansky V., Vega S. Polarization transfer dynamics in Lee-Goldburg cross polarization nuclear magnetic resonance experiments on rotating solids. J. Chem. Phys. 112:2000;7158-7168.
    • (2000) J. Chem. Phys. , vol.112 , pp. 7158-7168
    • Ladizhansky, V.1    Vega, S.2
  • 64
    • 48549111993 scopus 로고
    • Two-dimensional exchange NMR in rotating solids - A technique to study very slow molecular reorientations
    • Dejong A.F., Kentgens A.P.M., Veeman W.S. Two-dimensional exchange NMR in rotating solids - a technique to study very slow molecular reorientations. Chem. Phys. Lett. 109:1984;337-342.
    • (1984) Chem. Phys. Lett. , vol.109 , pp. 337-342
    • Dejong, A.F.1    Kentgens, A.P.M.2    Veeman, W.S.3
  • 65
    • 0033121307 scopus 로고    scopus 로고
    • Selective and extensive C-13 labeling of a membrane protein for solid-state NMR investigations
    • Hong M., Jakes K. Selective and extensive C-13 labeling of a membrane protein for solid-state NMR investigations. J. Biomol. NMR. 14:1999;71-74.
    • (1999) J. Biomol. NMR , vol.14 , pp. 71-74
    • Hong, M.1    Jakes, K.2
  • 67
    • 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. 159:2002;243-249.
    • (2002) J. Magn. Reson. , vol.159 , pp. 243-249
    • Luca, S.1    Baldus, M.2
  • 68
    • 45149145322 scopus 로고
    • Rotational-echo double-resonance NMR
    • Gullion T., Schaefer J. Rotational-echo double-resonance NMR. J. Magn. Reson. 81:1989;196-200.
    • (1989) J. Magn. Reson. , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 69
    • 0037063498 scopus 로고    scopus 로고
    • 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly C-13, N-15-labeled solids
    • Jaroniec C.P., Filip C., Griffin R.G. 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly C-13, N-15-labeled solids. J. Am. Chem. Soc. 124:2002;10728-10742.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10728-10742
    • Jaroniec, C.P.1    Filip, C.2    Griffin, R.G.3
  • 70
    • 84989629173 scopus 로고
    • Conformation-dependent C-13 chemical-shifts - A new means of conformational characterization as obtained by high-resolution solid-state C-13 NMR
    • Saito H. Conformation-dependent C-13 chemical-shifts - a new means of conformational characterization as obtained by high-resolution solid-state C-13 NMR. Magn. Reson. Chem. 24:1986;835-852.
    • (1986) Magn. Reson. Chem. , vol.24 , pp. 835-852
    • Saito, H.1
  • 71
    • 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. 20:2001;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
  • 72
    • 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. 124:2002;9704-9705.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9704-9705
    • Lange, A.1    Luca, S.2    Baldus, M.3
  • 73
    • 0141988942 scopus 로고    scopus 로고
    • Analysis of proton-proton transfer dynamics in rotating solids and their use for 3D structure determination
    • 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. 125:2003;12640-12648.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12640-12648
    • Lange, A.1    Seidel, K.2    Verdier, L.3    Luca, S.4    Baldus, M.5
  • 74
    • 0344393786 scopus 로고    scopus 로고
    • High-resolution solid-state NMR applied to polypeptides and membrane proteins
    • in press
    • S. Luca, H. Heise, M. Baldus, High-resolution solid-state NMR applied to polypeptides and membrane proteins, Acc. Chem. Res. (2003) in press.
    • (2003) Acc. Chem. Res.
    • Luca, S.1    Heise, H.2    Baldus, M.3
  • 75
    • 0030635055 scopus 로고    scopus 로고
    • Ambiguous distance data in the calculation of NMR structures
    • Nilges M. Ambiguous distance data in the calculation of NMR structures. Fold. Des. 2:1997;S53-S57.
    • (1997) Fold. Des. , vol.2
    • Nilges, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.