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Volumn 451, Issue , 2008, Pages 441-462

NMR analysis of viral protein structures

Author keywords

Chemical shift; NMR; Protein structure; Structural biology; Viruses

Indexed keywords


EID: 84934440490     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-102-4_30     Document Type: Article
Times cited : (13)

References (74)
  • 1
    • 28444480251 scopus 로고    scopus 로고
    • Comparisons of NMR spectral quality and success in crystallization demonstrate that NMR and X-ray crystallography are complementary methods for small protein structure determination
    • Snyder, D. A., Chen, Y., Denissova, N. G., Acton, T., Aramini, J. M., Ciano, M., et al. (2005) Comparisons of NMR spectral quality and success in crystallization demonstrate that NMR and X-ray crystallography are complementary methods for small protein structure determination. J. Am. Chem. Soc. 127, 16505-16511.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 16505-16511
    • Snyder, D.A.1    Chen, Y.2    Denissova, N.G.3    Acton, T.4    Aramini, J.M.5    Ciano, M.6
  • 2
    • 28444491122 scopus 로고    scopus 로고
    • NMR and X-ray crystallography, complementary tools in structural proteomics of small proteins
    • Yee, A. A., Savchenko, A., Ignachenko, A., Lukin, J., Xu, X., Skarina, T., et al. (2005) NMR and X-ray crystallography, complementary tools in structural proteomics of small proteins. J. Am. Chem. Soc. 127, 16512-16517.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 16512-16517
    • Yee, A.A.1    Savchenko, A.2    Ignachenko, A.3    Lukin, J.4    Xu, X.5    Skarina, T.6
  • 3
    • 0029109378 scopus 로고
    • NMR - this other method for protein and nucleic acid structure determination
    • Wuthrich, K. (1995) NMR - this other method for protein and nucleic acid structure determination. Acta Crystallogr. D Biol. Crystallogr. 51, 249-270.
    • (1995) Acta Crystallogr. D Biol. Crystallogr , vol.51 , pp. 249-270
    • Wuthrich, K.1
  • 4
    • 4644302181 scopus 로고    scopus 로고
    • NMR studies of partially folded molten-globule states
    • Redfield, C. (2004) NMR studies of partially folded molten-globule states. Methods Mol. Biol. 278, 233-254.
    • (2004) Methods Mol. Biol , vol.278 , pp. 233-254
    • Redfield, C.1
  • 5
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier, A. and Kay, L. E. (2006) New tools provide new insights in NMR studies of protein dynamics. Science 312, 224-228.
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 6
    • 20544455643 scopus 로고    scopus 로고
    • Ligand-target interactions: What can we learn from NMR?
    • Carlomagno, T. (2005) Ligand-target interactions: what can we learn from NMR? Annu. Rev. Biophys. Biomol. Struct. 34, 245-266.
    • (2005) Annu. Rev. Biophys. Biomol. Struct , vol.34 , pp. 245-266
    • Carlomagno, T.1
  • 7
    • 0022429237 scopus 로고
    • Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry
    • Williamson, M. P., Havel, T. F., and Wuthrich, K. (1985) Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry. J. Mol. Biol. 182, 295-315.
    • (1985) J. Mol. Biol , vol.182 , pp. 295-315
    • Williamson, M.P.1    Havel, T.F.2    Wuthrich, K.3
  • 8
    • 0037062977 scopus 로고    scopus 로고
    • NMR analysis of a 900K GroEL GroES complex
    • Fiaux, J., Bertelsen, E. B., Horwich, A. L., and Wuthrich, K. (2002) NMR analysis of a 900K GroEL GroES complex. Nature 418, 207-211.
    • (2002) Nature , vol.418 , pp. 207-211
    • Fiaux, J.1    Bertelsen, E.B.2    Horwich, A.L.3    Wuthrich, K.4
  • 9
    • 0037109010 scopus 로고    scopus 로고
    • Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy
    • Fernandez, C., Hilty, C., Wider, G., and Wuthrich, K. (2002) Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy. Proc. Natl. Acad. Sci. U S A 99, 13533-13537.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 13533-13537
    • Fernandez, C.1    Hilty, C.2    Wider, G.3    Wuthrich, K.4
  • 10
    • 33645473596 scopus 로고    scopus 로고
    • Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent exposed surface
    • Ahn, H. C., Juranic, N., Macura, S., and Markley, J. L. (2006) Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent exposed surface. J. Am. Chem. Soc. 128, 4398-4404.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 4398-4404
    • Ahn, H.C.1    Juranic, N.2    Macura, S.3    Markley, J.L.4
  • 11
    • 33645504750 scopus 로고    scopus 로고
    • NMR study of the tetrameric KcsA potassium channel in detergent micelles
    • Chill, J. H., Louis, J. M., Miller, C., and Bax, A. (2006) NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci. 15, 684-698.
    • (2006) Protein Sci , vol.15 , pp. 684-698
    • Chill, J.H.1    Louis, J.M.2    Miller, C.3    Bax, A.4
  • 12
    • 0028431597 scopus 로고
    • A novel isotope labeling protocol for bacterially expressed proteins
    • Reilly, D., and Fairbrother, W. J. (1994) A novel isotope labeling protocol for bacterially expressed proteins. J. Biomol. NMR 4, 459-462.
    • (1994) J. Biomol. NMR , vol.4 , pp. 459-462
    • Reilly, D.1    Fairbrother, W.J.2
  • 13
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • Cai, M., Huang, Y., Sakaguchi, K., Clore, G. M., Gronenborn, A. M., and Craigie, R. (1998) An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J. Biomol. NMR 11, 97-102.
    • (1998) J. Biomol. NMR , vol.11 , pp. 97-102
    • Cai, M.1    Huang, Y.2    Sakaguchi, K.3    Clore, G.M.4    Gronenborn, A.M.5    Craigie, R.6
  • 14
    • 0030735988 scopus 로고    scopus 로고
    • Solution NMR spectroscopy beyond 25 kDa
    • Kay, L. E. and Gardner, K. H. (1997) Solution NMR spectroscopy beyond 25 kDa. Curr. Opin. Struct. Biol. 7, 722-731.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 722-731
    • Kay, L.E.1    Gardner, K.H.2
  • 15
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • Goto, N. K. and Kay, L. E. (2000) New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr. Opin. Struct. Biol. 10, 585-592.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 16
    • 0034987544 scopus 로고    scopus 로고
    • A solubility- enhancement tag (SET) for NMR studies of poorly behaving proteins
    • Zhou, P., Lugovskoy, A. A., and Wagner, G. (2001) A solubility- enhancement tag (SET) for NMR studies of poorly behaving proteins. J. Biomol. NMR 20, 11-14.
    • (2001) J. Biomol. NMR , vol.20 , pp. 11-14
    • Zhou, P.1    Lugovskoy, A.A.2    Wagner, G.3
  • 17
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
    • Huth, J. R., Bewley, C. A., Jackson, B. M., Hinnebusch, A. G., Clore, G. M., and Gronenborn, A. M. (1997) Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci. 6, 2359-2364.
    • (1997) Protein Sci , vol.6 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3    Hinnebusch, A.G.4    Clore, G.M.5    Gronenborn, A.M.6
  • 18
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W. and Moffatt, B. A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130.
    • (1986) J. Mol. Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 20
    • 0000521134 scopus 로고
    • Spin-echo water suppression for the generation of pure-phase two-dimensional NMR Spectra
    • Sklenar, V. and Bax, A. (1987) Spin-echo water suppression for the generation of pure-phase two-dimensional NMR Spectra. J. Magn. Reson. 74, 469-479.
    • (1987) J. Magn. Reson , vol.74 , pp. 469-479
    • Sklenar, V.1    Bax, A.2
  • 21
    • 0025341339 scopus 로고
    • 15N spectra of proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin
    • 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry 29, 4659-4667.
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 22
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • Grzesiek, S. and Bax, A. (1992) Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96, 432-440.
    • (1992) J. Magn. Reson , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 23
    • 0026886847 scopus 로고
    • 1H alpha proton of the preceding residue
    • 1H alpha proton of the preceding residue. J. Biomol. NMR 2, 389-394.
    • (1992) J. Biomol. NMR , vol.2 , pp. 389-394
    • Clubb, R.T.1    Wagner, G.2
  • 25
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S. and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114, 6291-6293.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 27
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay, L. E., Ikura, M., Tschudin, R., and Bax, A. (1990) Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89, 496-514.
    • (1990) J. Magn. Reson , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 32
    • 0028803014 scopus 로고
    • Audio-frequency NMR in a nutating frame. Application to the assignment of phenylalanine residues in isotopically enriched proteins
    • Grzesiek, S. and Bax, A. (1995) Audio-frequency NMR in a nutating frame. Application to the assignment of phenylalanine residues in isotopically enriched proteins. J. Am. Chem. Soc. 117, 6527-6531.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 6527-6531
    • Grzesiek, S.1    Bax, A.2
  • 33
    • 33745356391 scopus 로고
    • Contact electron-spin coupling of nuclear magnetic moments
    • Karplus, M. (1959) Contact electron-spin coupling of nuclear magnetic moments. J. Chem. Phys. 30, 11-15.
    • (1959) J. Chem. Phys , vol.30 , pp. 11-15
    • Karplus, M.1
  • 34
    • 12044259775 scopus 로고    scopus 로고
    • 15N-enriched proteins. J. Am. Chem. Soc. 115, 7772-7777.
    • 15N-enriched proteins. J. Am. Chem. Soc. 115, 7772-7777.
  • 35
    • 0031062638 scopus 로고    scopus 로고
    • Grzesiek, S. and Bax, A. (1997) A three-dimensional NMR experiment with improved sensitivity for carbonyl-carbonyl J correlation in proteins. J. Biomol. NMR 9, 207-211.
    • Grzesiek, S. and Bax, A. (1997) A three-dimensional NMR experiment with improved sensitivity for carbonyl-carbonyl J correlation in proteins. J. Biomol. NMR 9, 207-211.
  • 36
    • 0034295408 scopus 로고    scopus 로고
    • Determination of backbone angle Ψ in proteins using a TROSY-based α/β-HN(CO)CA-J experiment
    • Permi, P., Kilpeläinen, I., and Annila, A. (2000) Determination of backbone angle Ψ in proteins using a TROSY-based α/β-HN(CO)CA-J experiment. J. Magn. Reson. 146, 255-259.
    • (2000) J. Magn. Reson , vol.146 , pp. 255-259
    • Permi, P.1    Kilpeläinen, I.2    Annila, A.3
  • 38
    • 0030981418 scopus 로고    scopus 로고
    • NC couplings. J. Am. Chem. Soc. 119, 1803-1804.
    • NC couplings. J. Am. Chem. Soc. 119, 1803-1804.
  • 40
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 42
    • 0033620446 scopus 로고    scopus 로고
    • Identification of the hydrogen bonding network in a protein by scalar couplings
    • Cornilescu, G., Hu, J.-S., and Bax, A. (1999) Identification of the hydrogen bonding network in a protein by scalar couplings. J. Am. Chem. Soc. 121, 2949-2950.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 2949-2950
    • Cornilescu, G.1    Hu, J.-S.2    Bax, A.3
  • 43
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra, N. and Bax, A. (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278, 1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 44
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • Bax, A. and Grishaev, A. (2005) Weak alignment NMR: a hawk-eyed view of biomolecular structure. Curr. Opin. Struct. Biol. 15, 563-570.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 45
    • 0032042263 scopus 로고    scopus 로고
    • Ottiger, M., Delaglio, F., and Bax, A. (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 131, 373-378.
    • Ottiger, M., Delaglio, F., and Bax, A. (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 131, 373-378.
  • 46
    • 0035131780 scopus 로고    scopus 로고
    • Simple multidimensional NMR experiments to obtain different types of one-bond dipolar couplings simultaneously
    • de Alba, E., Suzuki, M., and Tjandra, N. (2001) Simple multidimensional NMR experiments to obtain different types of one-bond dipolar couplings simultaneously. J. Biomol. NMR 19, 63-67.
    • (2001) J. Biomol. NMR , vol.19 , pp. 63-67
    • de Alba, E.1    Suzuki, M.2    Tjandra, N.3
  • 47
    • 0031063544 scopus 로고    scopus 로고
    • CH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra. J. Magn. Reson. 124, 512-515.
    • CH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra. J. Magn. Reson. 124, 512-515.
  • 48
    • 0037151670 scopus 로고    scopus 로고
    • 1H dipolar couplings in weakly aligned proteins
    • 1H dipolar couplings in weakly aligned proteins. J. Am. Chem. Soc. 124, 9672-9673.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 9672-9673
    • Wu, Z.1    Bax, A.2
  • 50
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 52
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278, 313-352.
    • (2004) Methods Mol. Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 53
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T.-H., Billeter, M., Güntert, P., and Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 5, 1-10.
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 54
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 57
    • 0032587512 scopus 로고    scopus 로고
    • Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation
    • Wood, M. J. and Komives, E. A. (1999) Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation. J. Biomol. NMR 13, 149-159.
    • (1999) J. Biomol. NMR , vol.13 , pp. 149-159
    • Wood, M.J.1    Komives, E.A.2
  • 58
    • 7044263294 scopus 로고    scopus 로고
    • Optimization of an Escherichia coli system for cell-free synthesis of selectively N-labeled proteins for rapid analysis by NMR spectroscopy
    • Ozawa, K., Headlam, M. J., Schaeffer, P. M., Henderson, B. R., Dixon, N. E., and Otting, G. (2004) Optimization of an Escherichia coli system for cell-free synthesis of selectively N-labeled proteins for rapid analysis by NMR spectroscopy. Eur. J. Biochem. 271, 4084-4093.
    • (2004) Eur. J. Biochem , vol.271 , pp. 4084-4093
    • Ozawa, K.1    Headlam, M.J.2    Schaeffer, P.M.3    Henderson, B.R.4    Dixon, N.E.5    Otting, G.6
  • 59
    • 14344256801 scopus 로고    scopus 로고
    • Cell-free protein production and labeling protocol for NMR-based structural proteomics
    • Vinarov, D. A., Lytle, B. L., Peterson, F. C., Tyler, E. M., Volkman, B. F., and Markley, J. L. (2004) Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat. Methods 1, 149-153.
    • (2004) Nat. Methods , vol.1 , pp. 149-153
    • Vinarov, D.A.1    Lytle, B.L.2    Peterson, F.C.3    Tyler, E.M.4    Volkman, B.F.5    Markley, J.L.6
  • 60
    • 14344255383 scopus 로고    scopus 로고
    • Vinarov, D. A. and Markley, J. L. (2005) High-throughput automated platform for nuclear magnetic resonance-based structural proteomics. Expert Rev. Proteomics 2, 49-55.
    • Vinarov, D. A. and Markley, J. L. (2005) High-throughput automated platform for nuclear magnetic resonance-based structural proteomics. Expert Rev. Proteomics 2, 49-55.
  • 61
    • 0037205759 scopus 로고    scopus 로고
    • NMR analysis of in vitro-synthesized proteins without purification: A high-throughput approach
    • Guignard, L., Ozawa, K., Pursglove, S. E., Otting, G., and Dixon, N. E. (2002) NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach. FEBS Lett. 524, 159-162.
    • (2002) FEBS Lett , vol.524 , pp. 159-162
    • Guignard, L.1    Ozawa, K.2    Pursglove, S.E.3    Otting, G.4    Dixon, N.E.5
  • 62
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • Waugh, D. S. (2005) Making the most of affinity tags. Trends Biotechnol. 23, 316-320.
    • (2005) Trends Biotechnol , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 63
    • 0018782084 scopus 로고
    • Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor
    • Wuthrich, K. and Wagner, G. (1979) Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor. J. Mol. Biol. 130, 1-18.
    • (1979) J. Mol. Biol , vol.130 , pp. 1-18
    • Wuthrich, K.1    Wagner, G.2
  • 64
    • 0034918477 scopus 로고    scopus 로고
    • Optimization of protein solubility and stability for protein nuclear magnetic resonance
    • Bagby, S., Tong, K. I., and Ikura, M. (2001) Optimization of protein solubility and stability for protein nuclear magnetic resonance. Methods Enzymol. 339, 20-41.
    • (2001) Methods Enzymol , vol.339 , pp. 20-41
    • Bagby, S.1    Tong, K.I.2    Ikura, M.3
  • 65
    • 0031243139 scopus 로고    scopus 로고
    • The button test: A small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR
    • Bagby, S., Tong, K. I., Liu, D., Alattia, J. R., and Ikura, M. (1997) The button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR. J. Biomol. NMR 10, 279-282.
    • (1997) J. Biomol. NMR , vol.10 , pp. 279-282
    • Bagby, S.1    Tong, K.I.2    Liu, D.3    Alattia, J.R.4    Ikura, M.5
  • 66
    • 0032201444 scopus 로고    scopus 로고
    • Microdrop screening: A rapid method to optimize solvent conditions for NMR spectroscopy of proteins
    • Lepre, C. A. and Moore, J. M. (1998) Microdrop screening: a rapid method to optimize solvent conditions for NMR spectroscopy of proteins. J. Biomol. NMR 12, 493-499.
    • (1998) J. Biomol. NMR , vol.12 , pp. 493-499
    • Lepre, C.A.1    Moore, J.M.2
  • 67
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri, A. S., Hinton, D. P., and Byrd, R. A. (1995) Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J. Am. Chem. Soc. 117, 7566-7567.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 68
    • 0029400890 scopus 로고
    • Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2
    • Dingley, A. J., Mackay, J. P., Chapman, B. E., Morris, M. B., Kuchel, P. W., Hambly, B. D., et al. (1995) Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: application to myosin light chain 2. J. Biomol. NMR 6, 321-328.
    • (1995) J. Biomol. NMR , vol.6 , pp. 321-328
    • Dingley, A.J.1    Mackay, J.P.2    Chapman, B.E.3    Morris, M.B.4    Kuchel, P.W.5    Hambly, B.D.6
  • 69
    • 0020711969 scopus 로고
    • Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes
    • Wagner, G. (1983) Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. Q. Rev. Biophys. 16, 1-57.
    • (1983) Q. Rev. Biophys , vol.16 , pp. 1-57
    • Wagner, G.1
  • 70
    • 4744344737 scopus 로고    scopus 로고
    • Automation of NMR structure determination of proteins
    • Altieri, A. S. and Byrd, R. A. (2004) Automation of NMR structure determination of proteins. Curr. Opin. Struct. Biol. 14, 547-553.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 547-553
    • Altieri, A.S.1    Byrd, R.A.2
  • 71
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., Riek, R., Wider, G., and Wuthrich, K. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. USA 94, 12366-12371.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 72
    • 0034919240 scopus 로고    scopus 로고
    • Automated assignment of ambiguous nuclear overhauser effects with ARIA
    • Linge, J. P., O'Donoghue, S. I., and Nilges, M. (2001) Automated assignment of ambiguous nuclear overhauser effects with ARIA. Methods Enzymol. 339, 71-90.
    • (2001) Methods Enzymol , vol.339 , pp. 71-90
    • Linge, J.P.1    O'Donoghue, S.I.2    Nilges, M.3
  • 73
    • 0036217249 scopus 로고    scopus 로고
    • Automated assignment and 3D structure calculations using combinations of 2D homonuclear and 3D heteronuclear NOESY spectra
    • Oezguen, N., Adamian, L., Xu, Y., Rajarathnam, K., and Braun, W. (2002) Automated assignment and 3D structure calculations using combinations of 2D homonuclear and 3D heteronuclear NOESY spectra. J. Biomol. NMR 22, 249-263.
    • (2002) J. Biomol. NMR , vol.22 , pp. 249-263
    • Oezguen, N.1    Adamian, L.2    Xu, Y.3    Rajarathnam, K.4    Braun, W.5
  • 74
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann, T., Guntert, P., and Wuthrich, K. (2002) Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J. Biomol. NMR 24, 171-189.
    • (2002) J. Biomol. NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3


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