메뉴 건너뛰기




Volumn 162, Issue 2, 2003, Pages 385-395

Internal consistency of NMR data obtained in partially aligned biomacromolecules

Author keywords

Chemical shift anisotropy; NMR; Nucleic acid base; Peptide plane; Residual dipolar couplings

Indexed keywords

ANISOTROPY; CHEMICAL BONDS; MACROMOLECULES; NUCLEIC ACIDS; TENSORS;

EID: 0042173200     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1090-7807(03)00116-2     Document Type: Article
Times cited : (14)

References (21)
  • 1
    • 0035591656 scopus 로고    scopus 로고
    • Residual dipolar couplings in protein NMR
    • Brunner E. Residual dipolar couplings in protein NMR. Concepts Magn. Reson. 13:2001;238-259.
    • (2001) Concepts Magn. Reson. , vol.13 , pp. 238-259
    • Brunner, E.1
  • 2
    • 0034792548 scopus 로고    scopus 로고
    • Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: An application to maltose binding protein
    • Choy W.Y., Tollinger M., Mueller G.A., Kay L.E. Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein. J. Biomol. NMR. 21:2001;31-40.
    • (2001) J. Biomol. NMR , vol.21 , pp. 31-40
    • Choy, W.Y.1    Tollinger, M.2    Mueller, G.A.3    Kay, L.E.4
  • 3
    • 0032113480 scopus 로고    scopus 로고
    • A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information
    • Clore G.M., Gronenborn A.M., Bax A. A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J. Magn. Reson. 133:1998;216-221.
    • (1998) J. Magn. Reson. , vol.133 , pp. 216-221
    • Clore, G.M.1    Gronenborn, A.M.2    Bax, A.3
  • 4
    • 0034684181 scopus 로고    scopus 로고
    • Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase
    • Cornilescu G., Bax A. Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase. J. Am. Chem. Soc. 122:2000;10143-10154.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10143-10154
    • Cornilescu, G.1    Bax, A.2
  • 5
    • 0037169646 scopus 로고    scopus 로고
    • NMR dipolar couplings for the structure determination of biopolymers in solution
    • de Alba E., Tjandra N. NMR dipolar couplings for the structure determination of biopolymers in solution. J. Biomol. NMR. 40:2002;175-197.
    • (2002) J. Biomol. NMR , vol.40 , pp. 175-197
    • De Alba, E.1    Tjandra, N.2
  • 6
    • 0030764469 scopus 로고    scopus 로고
    • 13C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond?
    • 13C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond? J. Am. Chem. Soc. 119:1996;6360-6368.
    • (1996) J. Am. Chem. Soc. , vol.119 , pp. 6360-6368
    • Hu, J.1    Bax, A.2
  • 7
    • 0035925135 scopus 로고    scopus 로고
    • Determination of protein backbone structure using only residual dipolar couplings
    • Hus J.C., Marion D., Blackledge M. Determination of protein backbone structure using only residual dipolar couplings. J. Am. Chem. Soc. 123:2001;1541-1542.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1541-1542
    • Hus, J.C.1    Marion, D.2    Blackledge, M.3
  • 8
    • 0033145058 scopus 로고    scopus 로고
    • Order matrix analysis of residual dipolar couplings using singular value decomposition
    • Losonczi J.A., Andrec M., Fischer M.W.F., Prestegard J.H. Order matrix analysis of residual dipolar couplings using singular value decomposition. J. Magn. Reson. 138:1999;334-342.
    • (1999) J. Magn. Reson. , vol.138 , pp. 334-342
    • Losonczi, J.A.1    Andrec, M.2    Fischer, M.W.F.3    Prestegard, J.H.4
  • 9
    • 0034072742 scopus 로고    scopus 로고
    • NMR solution structure determination of RNAs
    • Mollova E.T., Pardi A. NMR solution structure determination of RNAs. Curr. Opin. Struct. Biol. 10:2000;298-302.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 298-302
    • Mollova, E.T.1    Pardi, A.2
  • 10
    • 0032866940 scopus 로고    scopus 로고
    • Structural constraints from residual tensorial couplings in high resolution NMR without an explicit term for the alignment tensor
    • Moltke S., Grzesiek S. Structural constraints from residual tensorial couplings in high resolution NMR without an explicit term for the alignment tensor. J. Biomol. NMR. 15:1999;77-82.
    • (1999) J. Biomol. NMR , vol.15 , pp. 77-82
    • Moltke, S.1    Grzesiek, S.2
  • 11
    • 0034733394 scopus 로고    scopus 로고
    • Global folds of proteins with low densities of NOE using residual dipolar couplings: Application to the 370-residue maltodextrin-binding protein
    • Mueller G.A., Choy W.Y., Yang D.W., Forman-Kay J.D., Venters R.A., Kay L.E. Global folds of proteins with low densities of NOE using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein. J. Mol. Biol. 300:2000;197-212.
    • (2000) J. Mol. Biol. , vol.300 , pp. 197-212
    • Mueller, G.A.1    Choy, W.Y.2    Yang, D.W.3    Forman-Kay, J.D.4    Venters, R.A.5    Kay, L.E.6
  • 12
    • 0032477283 scopus 로고    scopus 로고
    • α effective bond lengths in a protein by NMR in a dilute liquid crystalline phase
    • α effective bond lengths in a protein by NMR in a dilute liquid crystalline phase J. Am. Chem. Soc. 120:1998;12334-12341.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12334-12341
    • Ottiger, M.1    Bax, A.2
  • 13
    • 0036755397 scopus 로고    scopus 로고
    • Refinement of d(GCGAAGC) hairpin structure using one- and two-bond residual dipolar couplings
    • Padrta P., Štefl R., Králík L., Žídek L., Sklenář V. Refinement of d(GCGAAGC) hairpin structure using one- and two-bond residual dipolar couplings. J. Biomol. NMR. 24:2002;1-14.
    • (2002) J. Biomol. NMR , vol.24 , pp. 1-14
    • Padrta, P.1    Štefl, R.2    Králík, L.3    Žídek, L.4    Sklenář, V.5
  • 14
    • 0034003170 scopus 로고    scopus 로고
    • Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings
    • Permi P., Annila A. Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings. J. Biomol. NMR. 16:2000;221-227.
    • (2000) J. Biomol. NMR , vol.16 , pp. 221-227
    • Permi, P.1    Annila, A.2
  • 15
    • 0036462497 scopus 로고    scopus 로고
    • De novo structure determination from residual dipolar couplings by NMR spectroscopy
    • Simon B., Sattler M. De novo structure determination from residual dipolar couplings by NMR spectroscopy. Angew. Chem.-Int. Ed. 41:2002;437-440.
    • (2002) Angew. Chem.-Int. Ed. , vol.41 , pp. 437-440
    • Simon, B.1    Sattler, M.2
  • 16
    • 0035443893 scopus 로고    scopus 로고
    • Dipolar couplings as a probe of molecular dynamics and structure in solution
    • Tolman J.R. Dipolar couplings as a probe of molecular dynamics and structure in solution. Curr. Opin. Struct. Biol. 11:2001;532-539.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 532-539
    • Tolman, J.R.1
  • 18
    • 0035154128 scopus 로고    scopus 로고
    • Measurement of small scalar and dipolar couplings in purine and pyrimidine bases
    • Žídek L., Wu H.H., Feigon J., Sklenář V. Measurement of small scalar and dipolar couplings in purine and pyrimidine bases. J. Biomol. NMR. 21:2001;153-160.
    • (2001) J. Biomol. NMR , vol.21 , pp. 153-160
    • Žídek, L.1    Wu, H.H.2    Feigon, J.3    Sklenář, V.4
  • 19
    • 0034741617 scopus 로고    scopus 로고
    • 31P chemical shift anisotropy as an aid in determining nucleic acid structure in liquid crystals
    • 31P chemical shift anisotropy as an aid in determining nucleic acid structure in liquid crystals J. Am. Chem. Soc. 123:2001;3617-3618.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3617-3618
    • Wu, Z.1    Tjandra, N.2    Bax, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.