메뉴 건너뛰기




Volumn 184, Issue 1, 2007, Pages 51-61

The influence of nitrogen-15 proton-driven spin diffusion on the measurement of nitrogen-15 longitudinal relaxation times

Author keywords

MAS; Relaxation

Indexed keywords

DIFFUSION; ERROR ANALYSIS; MAGNETIC RESONANCE; MAGNETIZATION; PARAMETER ESTIMATION; PROTEINS;

EID: 33846004467     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2006.09.015     Document Type: Article
Times cited : (54)

References (32)
  • 1
    • 33645834303 scopus 로고    scopus 로고
    • Review-New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier A., and Kay L.E. Review-New tools provide new insights in NMR studies of protein dynamics. Science 312 5771 (2006) 224-228
    • (2006) Science , vol.312 , Issue.5771 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 2
    • 84939988155 scopus 로고
    • Deuterium relaxation in molecular solids
    • Warren W.S. (Ed), Academic Press, New York
    • Vold R., and Vold R.L. Deuterium relaxation in molecular solids. In: Warren W.S. (Ed). Advances in Magnetic and Optical Resonance (1991), Academic Press, New York 85
    • (1991) Advances in Magnetic and Optical Resonance , pp. 85
    • Vold, R.1    Vold, R.L.2
  • 3
    • 0002210634 scopus 로고
    • Rotation of molecules and nuclear spin relaxation
    • Diehl P., Fluck E., and Kosfeld R. (Eds), Springer-Verlag, Berlin, Heidelberg, New York
    • Spiess H.W. Rotation of molecules and nuclear spin relaxation. In: Diehl P., Fluck E., and Kosfeld R. (Eds). NMR Basic Principles and Progress (1978), Springer-Verlag, Berlin, Heidelberg, New York 15
    • (1978) NMR Basic Principles and Progress , pp. 15
    • Spiess, H.W.1
  • 4
    • 0001535072 scopus 로고
    • An NMR study of the backbone dynamics of staphylococcal nuclease in the crystalline state
    • Cole H.B.R., and Torchia D. An NMR study of the backbone dynamics of staphylococcal nuclease in the crystalline state. Chem. Phys. 158 2-3 (1991) 271-281
    • (1991) Chem. Phys. , vol.158 , Issue.2-3 , pp. 271-281
    • Cole, H.B.R.1    Torchia, D.2
  • 5
    • 0028504496 scopus 로고
    • A solid-state H-2-Nmr investigation of purine motion in a 12-base-pair RNA duplex
    • Wang A.C., Kennedy M.A., Reid B.R., and Drobny G.P. A solid-state H-2-Nmr investigation of purine motion in a 12-base-pair RNA duplex. J. Magn. Reson. B 105 1 (1994) 1-10
    • (1994) J. Magn. Reson. B , vol.105 , Issue.1 , pp. 1-10
    • Wang, A.C.1    Kennedy, M.A.2    Reid, B.R.3    Drobny, G.P.4
  • 6
    • 0033988014 scopus 로고    scopus 로고
    • Backbone motions in a crystalline protein from field-dependent H-2-NMR relaxation and line-shape analysis
    • Mack J.W., Usha M.G., Long J., Griffin R.G., and Wittebort R.J. Backbone motions in a crystalline protein from field-dependent H-2-NMR relaxation and line-shape analysis. Biopolymers 53 1 (2000) 9-18
    • (2000) Biopolymers , vol.53 , Issue.1 , pp. 9-18
    • Mack, J.W.1    Usha, M.G.2    Long, J.3    Griffin, R.G.4    Wittebort, R.J.5
  • 7
    • 0035967901 scopus 로고    scopus 로고
    • The time scale of the catalytic loop motion in triosephosphate isomerase
    • Rozovsky S., and McDermott A.E. The time scale of the catalytic loop motion in triosephosphate isomerase. J. Mol. Biol. 310 1 (2001) 259-270
    • (2001) J. Mol. Biol. , vol.310 , Issue.1 , pp. 259-270
    • Rozovsky, S.1    McDermott, A.E.2
  • 8
    • 4544369426 scopus 로고    scopus 로고
    • Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy
    • Giraud N., Böckmann A., Lesage A., Penin F., Blackledge M., and Emsley L. Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy. J. Am. Chem. Soc. 126 37 (2004) 11422-11423
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.37 , pp. 11422-11423
    • Giraud, N.1    Böckmann, A.2    Lesage, A.3    Penin, F.4    Blackledge, M.5    Emsley, L.6
  • 9
    • 29844444039 scopus 로고    scopus 로고
    • Quantitative analysis of backbone dynamics in a crystalline protein from nitrogen-15 spin-lattice relaxation
    • Giraud N., Blackledge M., Goldman M., Böckmann A., Lesage A., Penin F., and Emsley L. Quantitative analysis of backbone dynamics in a crystalline protein from nitrogen-15 spin-lattice relaxation. J. Am. Chem. Soc. 127 51 (2005) 18190-18201
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.51 , pp. 18190-18201
    • Giraud, N.1    Blackledge, M.2    Goldman, M.3    Böckmann, A.4    Lesage, A.5    Penin, F.6    Emsley, L.7
  • 10
    • 33645875338 scopus 로고    scopus 로고
    • Characterization of dynamic processes using deuterium in uniformly H-2, C-13, N-15 enriched peptides by MAS solid-state NMR
    • Hologne M., Chen Z.J., and Reif B. Characterization of dynamic processes using deuterium in uniformly H-2, C-13, N-15 enriched peptides by MAS solid-state NMR. J. Magn. Reson. 179 1 (2006) 20-28
    • (2006) J. Magn. Reson. , vol.179 , Issue.1 , pp. 20-28
    • Hologne, M.1    Chen, Z.J.2    Reif, B.3
  • 11
    • 49049140501 scopus 로고
    • Spin-lattice relaxation in solids
    • Torchia D., and Szabo A. Spin-lattice relaxation in solids. J. Magn. Reson. 49 (1982) 107-121
    • (1982) J. Magn. Reson. , vol.49 , pp. 107-121
    • Torchia, D.1    Szabo, A.2
  • 12
    • 0000420376 scopus 로고
    • Spin-lattice relaxation of C-13 in solid amino-acids using the Cp-Mas technique
    • Naito A., Ganapathy S., Akasaka K., and McDowell C.A. Spin-lattice relaxation of C-13 in solid amino-acids using the Cp-Mas technique. J. Magn. Reson. 54 2 (1983) 226-235
    • (1983) J. Magn. Reson. , vol.54 , Issue.2 , pp. 226-235
    • Naito, A.1    Ganapathy, S.2    Akasaka, K.3    McDowell, C.A.4
  • 13
    • 0001739017 scopus 로고
    • On the interaction of nuclear spins in a crystalline lattice
    • Bloembergen N. On the interaction of nuclear spins in a crystalline lattice. Physica 15 3-4 (1949) 386-426
    • (1949) Physica , vol.15 , Issue.3-4 , pp. 386-426
    • Bloembergen, N.1
  • 15
    • 0001618315 scopus 로고
    • Spin diffusion in resolved solid-state NMR-spectra
    • Suter D., and Ernst R.R. Spin diffusion in resolved solid-state NMR-spectra. Phys. Rev. B 32 9 (1985) 5608-5627
    • (1985) Phys. Rev. B , vol.32 , Issue.9 , pp. 5608-5627
    • Suter, D.1    Ernst, R.R.2
  • 16
    • 36549091295 scopus 로고
    • Dynamics of the C-13 spin-exchange process in solids-a theoretical and experimental-study
    • Henrichs P.M., Linder M., and Hewitt J.M. Dynamics of the C-13 spin-exchange process in solids-a theoretical and experimental-study. J. Chem. Phys. 85 12 (1986) 7077-7086
    • (1986) J. Chem. Phys. , vol.85 , Issue.12 , pp. 7077-7086
    • Henrichs, P.M.1    Linder, M.2    Hewitt, J.M.3
  • 17
    • 0002528855 scopus 로고
    • Polarization transfer and spin diffusion in solid-state
    • Meier B.H. Polarization transfer and spin diffusion in solid-state. Adv. Magn. Opt. Reson. 18 (1994) 1
    • (1994) Adv. Magn. Opt. Reson. , vol.18 , pp. 1
    • Meier, B.H.1
  • 19
    • 37049070374 scopus 로고
    • Spectral spin diffusion in polycrystalline solids under magic-angle spinning
    • Kubo A., and McDowell C.A. Spectral spin diffusion in polycrystalline solids under magic-angle spinning. J. Chem. Soc. Faraday Trans. I 84 (1988) 3713-3730
    • (1988) J. Chem. Soc. Faraday Trans. I , vol.84 , pp. 3713-3730
    • Kubo, A.1    McDowell, C.A.2
  • 20
    • 0037038365 scopus 로고    scopus 로고
    • Structure of protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • Castellani F., van Rossum B., Diehl A., Schubert M., Rehbein K., and Oschkinat H. Structure of 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
  • 22
    • 0037433237 scopus 로고    scopus 로고
    • Characterization of H-1-H-1 distances in a uniformly H-2,N-15-labeled SH3 domain by MAS solid-state NMR spectroscopy
    • Reif B., van Rossum B.J., Castellani F., Rehbein K., Diehl A., and Oschkinat H. Characterization of H-1-H-1 distances in a uniformly H-2,N-15-labeled SH3 domain by MAS solid-state NMR spectroscopy. J. Am. Chem. Soc. 125 6 (2003) 1488-1489
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.6 , pp. 1488-1489
    • Reif, B.1    van Rossum, B.J.2    Castellani, F.3    Rehbein, K.4    Diehl, A.5    Oschkinat, H.6
  • 23
    • 21244479996 scopus 로고    scopus 로고
    • Powder crystallography by proton solid-state NMR spectroscopy
    • Elena B., and Emsley L. Powder crystallography by proton solid-state NMR spectroscopy. J. Am. Chem. Soc. 127 25 (2005) 9140-9146
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.25 , pp. 9140-9146
    • Elena, B.1    Emsley, L.2
  • 24
    • 0042326473 scopus 로고    scopus 로고
    • Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue HPr
    • Juy M., Penin F., Favier A., Galinier A., Montserret R., Haser R., Deutscher J., and Böckmann A. Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue HPr. J. Mol. Biol. 332 (2003) 767-776
    • (2003) J. Mol. Biol. , vol.332 , pp. 767-776
    • Juy, M.1    Penin, F.2    Favier, A.3    Galinier, A.4    Montserret, R.5    Haser, R.6    Deutscher, J.7    Böckmann, A.8
  • 25
    • 0141483325 scopus 로고    scopus 로고
    • Determination of solid-state NMR structures of proteins by means of three-dimensional N-15-C-13-C-13 dipolar correlation spectroscopy and chemical shift analysis
    • Castellani F., van Rossum B.J., Diehl A., Rehbein K., and Oschkinat H. Determination of solid-state NMR structures of proteins by means of three-dimensional N-15-C-13-C-13 dipolar correlation spectroscopy and chemical shift analysis. Biochemistry 42 39 (2003) 11476-11483
    • (2003) Biochemistry , vol.42 , Issue.39 , pp. 11476-11483
    • Castellani, F.1    van Rossum, B.J.2    Diehl, A.3    Rehbein, K.4    Oschkinat, H.5
  • 26
    • 4244050504 scopus 로고    scopus 로고
    • Solid state NMR sequential resonance assignments and conformational analysis of the 2 × 104 kDa dimeric form of the Bacillus subtilis protein Crh
    • Böckmann A., Lange A., Galinier A., Luca S., Giraud N., Juy M., Heise H., Montserret R., Penin F., and Baldus M. Solid state NMR sequential resonance assignments and conformational analysis of the 2 × 104 kDa dimeric form of the Bacillus subtilis protein Crh. J. Biomol. NMR 27 4 (2003) 323-339
    • (2003) J. Biomol. NMR , vol.27 , Issue.4 , pp. 323-339
    • Böckmann, A.1    Lange, A.2    Galinier, A.3    Luca, S.4    Giraud, N.5    Juy, M.6    Heise, H.7    Montserret, R.8    Penin, F.9    Baldus, M.10
  • 27
    • 84915716471 scopus 로고
    • Elucidation of cross relaxation in liquids by two-dimensional NMR-spectroscopy
    • Macura S., and Ernst R.R. Elucidation of cross relaxation in liquids by two-dimensional NMR-spectroscopy. Mol. Phys. 41 1 (1980) 95-117
    • (1980) Mol. Phys. , vol.41 , Issue.1 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 28
    • 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., and Baldus M. Analysis of proton-proton transfer dynamics in rotating solids and their use for 3D structure determination. J. Am. Chem. Soc. 125 41 (2003) 12640-12648
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.41 , pp. 12640-12648
    • Lange, A.1    Seidel, K.2    Verdier, L.3    Luca, S.4    Baldus, M.5
  • 29
    • 33845980988 scopus 로고    scopus 로고
    • Maplesoft Maple, 9.50, 2004.
  • 30
    • 0242267593 scopus 로고    scopus 로고
    • Water-protein interactions in microcrystalline Crh measured by H-1-C-13 solid-state NMR spectroscopy
    • Lesage A., and Böckmann A. Water-protein interactions in microcrystalline Crh measured by H-1-C-13 solid-state NMR spectroscopy. J. Am. Chem. Soc. 125 44 (2003) 13336-13337
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.44 , pp. 13336-13337
    • Lesage, A.1    Böckmann, A.2
  • 31
    • 24344499503 scopus 로고    scopus 로고
    • Water-protein hydrogen exchange in the micro-crystalline protein Crh as observed by solid state NMR spectroscopy
    • Böckmann A., Juy M., Bettler E., Emsley L., Galinier A., Penin F., and Lesage A. Water-protein hydrogen exchange in the micro-crystalline protein Crh as observed by solid state NMR spectroscopy. J. Biomol. NMR 32 3 (2005) 195-207
    • (2005) J. Biomol. NMR , vol.32 , Issue.3 , pp. 195-207
    • Böckmann, A.1    Juy, M.2    Bettler, E.3    Emsley, L.4    Galinier, A.5    Penin, F.6    Lesage, A.7
  • 32
    • 33745676528 scopus 로고    scopus 로고
    • Investigation of dipolar-mediated water-protein interactions in microcrystalline Crh by solid-state NMR spectroscopy
    • Lesage A., Emsley L., Penin F., and Böckmann A. Investigation of dipolar-mediated water-protein interactions in microcrystalline Crh by solid-state NMR spectroscopy. J. Am. Chem. Soc. 128 25 (2006) 8246-8255
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.25 , pp. 8246-8255
    • Lesage, A.1    Emsley, L.2    Penin, F.3    Böckmann, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.