메뉴 건너뛰기




Volumn 430, Issue , 2007, Pages 283-331

NMR Methods for Studying Protein-Protein Interactions Involved in Translation Initiation

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTIC METHOD; CARBON NUCLEAR MAGNETIC RESONANCE; MOLECULAR DYNAMICS; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN RNA BINDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REVIEW; TECHNOLOGY; TRANSLATION INITIATION; ARTICLE; BIOLOGICAL MODEL; CHEMISTRY; ISOTOPE LABELING; MACROMOLECULE; METABOLISM; METHODOLOGY; PROTEIN BINDING; PROTEIN CONFORMATION; RNA TRANSLATION;

EID: 38449103508     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)30012-8     Document Type: Chapter
Times cited : (49)

References (109)
  • 1
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., and Schwede T. The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22 (2006) 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 2
    • 0012792234 scopus 로고    scopus 로고
    • Global fold determination of large proteins using site-directed spin labeling
    • Krishna N.R., and Berliner L.J. (Eds), Kluwer Academic/Plenum Publishers, New York
    • Battiste J.L., Gross J.D., and Wagner G. Global fold determination of large proteins using site-directed spin labeling. In: Krishna N.R., and Berliner L.J. (Eds). "Protein NMR for the Millennium" Vol. 20 (2003), Kluwer Academic/Plenum Publishers, New York 79-101
    • (2003) "Protein NMR for the Millennium" , vol.20 , pp. 79-101
    • Battiste, J.L.1    Gross, J.D.2    Wagner, G.3
  • 3
    • 0033963789 scopus 로고    scopus 로고
    • The eIF1A solution structure reveals a large RNA-binding surface important for scanning function
    • Battiste J.L., Pestova T.V., Hellen C.U., and Wagner G. The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. Mol. Cell 5 (2000) 109-119
    • (2000) Mol. Cell , vol.5 , pp. 109-119
    • Battiste, J.L.1    Pestova, T.V.2    Hellen, C.U.3    Wagner, G.4
  • 4
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data
    • Battiste J.L., and Wagner G. Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data. Biochemistry 39 (2000) 5355-5365
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 5
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • Bax A. Weak alignment offers new NMR opportunities to study protein structure and dynamics. Protein Sci. 12 (2003) 1-16
    • (2003) Protein Sci. , vol.12 , pp. 1-16
    • Bax, A.1
  • 6
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • Bax A., and Grishaev A. Weak alignment NMR: A hawk-eyed view of biomolecular structure. Curr. Opin. Struct. Biol. 15 (2005) 563-570
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 7
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G., and Ruben D.J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69 (1980) 185-189
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 8
    • 33845203743 scopus 로고    scopus 로고
    • Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings
    • Bouvignies G., Markwick P., Bruschweiler R., and Blackledge M. Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings. J. Am. Chem. Soc. 128 (2006) 15100-15101
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15100-15101
    • Bouvignies, G.1    Markwick, P.2    Bruschweiler, R.3    Blackledge, M.4
  • 9
    • 0042933782 scopus 로고    scopus 로고
    • De novo determination of bond orientations and order parameters from residual dipolar couplings with high accuracy
    • Briggman K.B., and Tolman J.R. De novo determination of bond orientations and order parameters from residual dipolar couplings with high accuracy. J. Am. Chem. Soc. 125 (2003) 10164-10165
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10164-10165
    • Briggman, K.B.1    Tolman, J.R.2
  • 11
    • 0037398803 scopus 로고    scopus 로고
    • New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins
    • Bruschweiler R. New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins. Curr. Opin. Struct. Biol. 13 (2003) 175-183
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 175-183
    • Bruschweiler, R.1
  • 12
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Bruschweiler R., Liao X., and Wright P.E. Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science 268 (1995) 886-889
    • (1995) Science , vol.268 , pp. 886-889
    • Bruschweiler, R.1    Liao, X.2    Wright, P.E.3
  • 13
    • 11144357574 scopus 로고    scopus 로고
    • Covariance nuclear magnetic resonance spectroscopy
    • Bruschweiler R., and Zhang F. Covariance nuclear magnetic resonance spectroscopy. J. Chem. Phys. 120 (2004) 5253-5260
    • (2004) J. Chem. Phys. , vol.120 , pp. 5253-5260
    • Bruschweiler, R.1    Zhang, F.2
  • 14
    • 49349130990 scopus 로고
    • Spin-spin couplings and the conformational states of peptide systems
    • Bystrov N.S. Spin-spin couplings and the conformational states of peptide systems. Progr. Nucl. Magn. Res. Spectrosc. 10 (1976) 41-81
    • (1976) Progr. Nucl. Magn. Res. Spectrosc. , vol.10 , pp. 41-81
    • Bystrov, N.S.1
  • 15
    • 0036283096 scopus 로고    scopus 로고
    • Molecular dynamics and NMR spin relaxation in proteins
    • Case D.A. Molecular dynamics and NMR spin relaxation in proteins. Acc. Chem. Res. 35 (2002) 325-331
    • (2002) Acc. Chem. Res. , vol.35 , pp. 325-331
    • Case, D.A.1
  • 16
    • 0037035528 scopus 로고    scopus 로고
    • Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: A representative of the eIF2beta/eIF5 family of proteins
    • Cho S., and Hoffman D.W. Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: A representative of the eIF2beta/eIF5 family of proteins. Biochemistry 41 (2002) 5730-5742
    • (2002) Biochemistry , vol.41 , pp. 5730-5742
    • Cho, S.1    Hoffman, D.W.2
  • 18
    • 0037433504 scopus 로고    scopus 로고
    • Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics
    • Clore G.M., and Schwieters C.D. Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics. J. Am. Chem. Soc. 125 (2003) 2902-2912
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2902-2912
    • Clore, G.M.1    Schwieters, C.D.2
  • 19
    • 33645677012 scopus 로고    scopus 로고
    • Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors
    • 4458
    • Conte M.R., Kelly G., Babon J., Sanfelice D., Youell J., Smerdon S.J., and Proud C.G. Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors. Biochemistry 45 (2006) 4550 4458
    • (2006) Biochemistry , vol.45 , pp. 4550
    • Conte, M.R.1    Kelly, G.2    Babon, J.3    Sanfelice, D.4    Youell, J.5    Smerdon, S.J.6    Proud, C.G.7
  • 20
    • 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. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 21
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C., Boelens R., and Bonvin A.M. HADDOCK: A protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125 (2003) 1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 22
    • 0038675927 scopus 로고    scopus 로고
    • New approaches to structure determination by NMR spectroscopy
    • Dotsch V., and Wagner G. New approaches to structure determination by NMR spectroscopy. Curr. Opin. Struct. Biol. 8 (1998) 619-623
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 619-623
    • Dotsch, V.1    Wagner, G.2
  • 23
    • 34247241059 scopus 로고    scopus 로고
    • Structure of eIF3b-RRM and its interaction with eIF3j: Structural insights into the recruitment of eIF3b to the 40S ribosomal subunit
    • Elantak L., Tzakos A.G., Locker N., and Lukavsky P.J. Structure of eIF3b-RRM and its interaction with eIF3j: Structural insights into the recruitment of eIF3b to the 40S ribosomal subunit. J. Biol. Chem. 282 (2006) 8165-8174
    • (2006) J. Biol. Chem. , vol.282 , pp. 8165-8174
    • Elantak, L.1    Tzakos, A.G.2    Locker, N.3    Lukavsky, P.J.4
  • 24
    • 0037138706 scopus 로고    scopus 로고
    • TreeDock: A tool for protein docking based on minimizing van der Waals energies
    • Fahmy A., and Wagner G. TreeDock: A tool for protein docking based on minimizing van der Waals energies. J. Am. Chem. Soc. 124 (2002) 1241-1250
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1241-1250
    • Fahmy, A.1    Wagner, G.2
  • 25
    • 0000195125 scopus 로고
    • Simultaneous [13C,15N]-HMQC, A pseudo-triple resonance experiment
    • Farmer II B. Simultaneous [13C,15N]-HMQC, A pseudo-triple resonance experiment. J. Magn. Reson. 93 (1991) 635-641
    • (1991) J. Magn. Reson. , vol.93 , pp. 635-641
    • Farmer II, B.1
  • 26
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy: A multifaceted approach to macromolecular structure
    • Ferentz A.E., and Wagner G. NMR spectroscopy: A multifaceted approach to macromolecular structure. Q. Rev. Biophys. 33 (2000) 29-65
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 27
    • 0033551495 scopus 로고    scopus 로고
    • Domain orientation and dynamics in multidomain proteins from residual dipolar couplings
    • Fischer M.W., Losonczi J.A., Weaver J.L., and Prestegard J.H. Domain orientation and dynamics in multidomain proteins from residual dipolar couplings. Biochemistry 38 (1999) 9013-9022
    • (1999) Biochemistry , vol.38 , pp. 9013-9022
    • Fischer, M.W.1    Losonczi, J.A.2    Weaver, J.L.3    Prestegard, J.H.4
  • 28
    • 0042666838 scopus 로고    scopus 로고
    • Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B
    • Fleming K., Ghuman J., Yuan X., Simpson P., Szendroi A., Matthews S., and Curry S. Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B. Biochemistry 42 (2003) 8966-8975
    • (2003) Biochemistry , vol.42 , pp. 8966-8975
    • Fleming, K.1    Ghuman, J.2    Yuan, X.3    Simpson, P.4    Szendroi, A.5    Matthews, S.6    Curry, S.7
  • 29
    • 0033522507 scopus 로고    scopus 로고
    • Structure and interactions of the translation initiation factor eIF1
    • Fletcher C.M., Pestova T.V., Hellen C.U., and Wagner G. Structure and interactions of the translation initiation factor eIF1. EMBO J. 18 (1999) 2631-2637
    • (1999) EMBO J. , vol.18 , pp. 2631-2637
    • Fletcher, C.M.1    Pestova, T.V.2    Hellen, C.U.3    Wagner, G.4
  • 30
    • 31444432912 scopus 로고    scopus 로고
    • Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment
    • Frueh D.P., Arthanari H., and Wagner G. Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment. J. Biomol. NMR 33 (2005) 187-196
    • (2005) J. Biomol. NMR , vol.33 , pp. 187-196
    • Frueh, D.P.1    Arthanari, H.2    Wagner, G.3
  • 31
    • 33646574966 scopus 로고    scopus 로고
    • Non-uniformly sampled double-TROSY hNcaNH experiments for NMR sequential assignments of large proteins
    • Frueh D.P., Sun Z.Y., Vosburg D.A., Walsh C.T., Hoch J.C., and Wagner G. Non-uniformly sampled double-TROSY hNcaNH experiments for NMR sequential assignments of large proteins. J. Am. Chem. Soc. 128 (2006) 5757-5763
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5757-5763
    • Frueh, D.P.1    Sun, Z.Y.2    Vosburg, D.A.3    Walsh, C.T.4    Hoch, J.C.5    Wagner, G.6
  • 32
    • 33644531581 scopus 로고    scopus 로고
    • Determination of all NOES in 1H-13C-Me-ILV-U-2H-15N proteins with two time-shared experiments
    • Frueh D.P., Vosburg D.A., Walsh C.T., and Wagner G. Determination of all NOES in 1H-13C-Me-ILV-U-2H-15N proteins with two time-shared experiments. J. Biomol. NMR 34 (2006) 31-40
    • (2006) J. Biomol. NMR , vol.34 , pp. 31-40
    • Frueh, D.P.1    Vosburg, D.A.2    Walsh, C.T.3    Wagner, G.4
  • 33
    • 2942544364 scopus 로고    scopus 로고
    • Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements
    • Fushman D., Varadan R., Assfalg M., and Walker O. Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements. Progr. NMR Spectrosc. 44 (2004) 189-214
    • (2004) Progr. NMR Spectrosc. , vol.44 , pp. 189-214
    • Fushman, D.1    Varadan, R.2    Assfalg, M.3    Walker, O.4
  • 34
    • 0028988076 scopus 로고
    • 1H and 15N resonance assignments and structure of the N-terminal domain of Escherichia coli initiation factor 3
    • Garcia C., Fortier P.L., Blanquet S., Lallemand J.Y., and Dardel F. 1H and 15N resonance assignments and structure of the N-terminal domain of Escherichia coli initiation factor 3. Eur. J. Biochem. 228 (1995) 395-402
    • (1995) Eur. J. Biochem. , vol.228 , pp. 395-402
    • Garcia, C.1    Fortier, P.L.2    Blanquet, S.3    Lallemand, J.Y.4    Dardel, F.5
  • 35
    • 0028849240 scopus 로고
    • Solution structure of the ribosome-binding domain of E. coli translation initiation factor IF3. Homology with the U1A protein of the eukaryotic spliceosome
    • Garcia C., Fortier P.L., Blanquet S., Lallemand J.Y., and Dardel F. Solution structure of the ribosome-binding domain of E. coli translation initiation factor IF3. Homology with the U1A protein of the eukaryotic spliceosome. J. Mol. Biol. 254 (1995) 247-259
    • (1995) J. Mol. Biol. , vol.254 , pp. 247-259
    • Garcia, C.1    Fortier, P.L.2    Blanquet, S.3    Lallemand, J.Y.4    Dardel, F.5
  • 36
    • 0031595590 scopus 로고    scopus 로고
    • The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins
    • Gardner K.H., and Kay L.E. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct. 27 (1998) 357-406
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 37
    • 0031027910 scopus 로고    scopus 로고
    • Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR
    • Gardner K.H., Rosen M.K., and Kay L.E. Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. Biochemistry 36 (1997) 1389-1401
    • (1997) Biochemistry , vol.36 , pp. 1389-1401
    • Gardner, K.H.1    Rosen, M.K.2    Kay, L.E.3
  • 38
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • Goto N.K., and Kay L.E. New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr. Opin. Struct. Biol. 10 (2000) 585-592
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 39
    • 0037354160 scopus 로고    scopus 로고
    • A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes
    • Gross J.D., Gelev V.M., and Wagner G. A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes. J. Biomol. NMR 25 (2003) 235-242
    • (2003) J. Biomol. NMR , vol.25 , pp. 235-242
    • Gross, J.D.1    Gelev, V.M.2    Wagner, G.3
  • 41
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization
    • Grzesiek S., Anglister J., and Bax A. Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization. JMRB 101 (1992) 114-119
    • (1992) JMRB , vol.101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 42
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Guntert P. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278 (2004) 353-378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 43
    • 1342331856 scopus 로고    scopus 로고
    • Structure of the archaeal translation initiation factor aIF2 beta from Methanobacterium thermoautotrophicum: Implications for translation initiation
    • Gutierrez P., Osborne M.J., Siddiqui N., Trempe J.F., Arrowsmith C., and Gehring K. Structure of the archaeal translation initiation factor aIF2 beta from Methanobacterium thermoautotrophicum: Implications for translation initiation. Protein Sci. 13 (2004) 659-667
    • (2004) Protein Sci. , vol.13 , pp. 659-667
    • Gutierrez, P.1    Osborne, M.J.2    Siddiqui, N.3    Trempe, J.F.4    Arrowsmith, C.5    Gehring, K.6
  • 44
    • 0026225733 scopus 로고
    • 13C-labeled protein using constant-time evolution
    • 13C-labeled protein using constant-time evolution. J. Biomol. NMR 1 (1991) 299-304
    • (1991) J. Biomol. NMR , vol.1 , pp. 299-304
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 45
    • 4444333127 scopus 로고    scopus 로고
    • Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B
    • Ito T., Marintchev A., and Wagner G. Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. Structure (Camb) 12 (2004) 1693-1704
    • (2004) Structure (Camb) , vol.12 , pp. 1693-1704
    • Ito, T.1    Marintchev, A.2    Wagner, G.3
  • 46
    • 0037432325 scopus 로고    scopus 로고
    • Nature of full-length HMGB1 binding to cisplatin-modified DNA
    • Jung Y., and Lippard S.J. Nature of full-length HMGB1 binding to cisplatin-modified DNA. Biochemistry 42 (2003) 2664-2671
    • (2003) Biochemistry , vol.42 , pp. 2664-2671
    • Jung, Y.1    Lippard, S.J.2
  • 47
    • 0030749281 scopus 로고    scopus 로고
    • Isotope labelling of macromolecules for structural determinations
    • Kainosho M. Isotope labelling of macromolecules for structural determinations. Nat. Struct. Biol. 4 Suppl. (1997) 858-861
    • (1997) Nat. Struct. Biol. , vol.4 , Issue.SUPPL , pp. 858-861
    • Kainosho, M.1
  • 49
    • 14844361989 scopus 로고    scopus 로고
    • NMR studies of protein structure and dynamics
    • Kay L.E. NMR studies of protein structure and dynamics. J. Magn. Reson. 173 (2005) 193-207
    • (2005) J. Magn. Reson. , vol.173 , pp. 193-207
    • Kay, L.E.1
  • 50
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay L.E., Ikura M., Tschudin R., and Bax A. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89 (1990) 496-514
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 52
    • 33746256604 scopus 로고    scopus 로고
    • Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins
    • Koglin A., Klammt C., Trbovic N., Schwarz D., Schneider B., Schafer B., Lohr F., Bernhard F., and Dotsch V. Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins. Magn. Reson. Chem. 44 Spec. No. (2006) S17-S23
    • (2006) Magn. Reson. Chem. , vol.44 , Issue.Spec
    • Koglin, A.1    Klammt, C.2    Trbovic, N.3    Schwarz, D.4    Schneider, B.5    Schafer, B.6    Lohr, F.7    Bernhard, F.8    Dotsch, V.9
  • 53
    • 0034146355 scopus 로고    scopus 로고
    • Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times
    • Kontaxis G., Clore G.M., and Bax A. Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times. J. Magn. Reson. 143 (2000) 184-196
    • (2000) J. Magn. Reson. , vol.143 , pp. 184-196
    • Kontaxis, G.1    Clore, G.M.2    Bax, A.3
  • 56
    • 0242498378 scopus 로고    scopus 로고
    • Projection-reconstruction of three-dimensional NMR spectra
    • Kupce E., and Freeman R. Projection-reconstruction of three-dimensional NMR spectra. J. Am. Chem. Soc. 125 (2003) 13958-13959
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13958-13959
    • Kupce, E.1    Freeman, R.2
  • 57
    • 0042415779 scopus 로고    scopus 로고
    • Two-dimensional Hadamard spectroscopy
    • Kupce E., and Freeman R. Two-dimensional Hadamard spectroscopy. J. Magn. Reson. 162 (2003) 300-310
    • (2003) J. Magn. Reson. , vol.162 , pp. 300-310
    • Kupce, E.1    Freeman, R.2
  • 58
    • 0346733331 scopus 로고    scopus 로고
    • The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker
    • Laursen B.S., Kjaergaard A.C., Mortensen K.K., Hoffman D.W., and Sperling-Petersen H.U. The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker. Protein Sci. 13 (2004) 230-239
    • (2004) Protein Sci. , vol.13 , pp. 230-239
    • Laursen, B.S.1    Kjaergaard, A.C.2    Mortensen, K.K.3    Hoffman, D.W.4    Sperling-Petersen, H.U.5
  • 59
    • 0038182530 scopus 로고    scopus 로고
    • A conserved structural motif at the N terminus of bacterial translation initiation factor IF2
    • Laursen B.S., Mortensen K.K., Sperling-Petersen H.U., and Hoffman D.W. A conserved structural motif at the N terminus of bacterial translation initiation factor IF2. J. Biol. Chem. 278 (2003) 16320-16328
    • (2003) J. Biol. Chem. , vol.278 , pp. 16320-16328
    • Laursen, B.S.1    Mortensen, K.K.2    Sperling-Petersen, H.U.3    Hoffman, D.W.4
  • 60
    • 0035188225 scopus 로고    scopus 로고
    • Structure and dynamics of translation initiation factor aIF-1A from the archaeon Methanococcus jannaschii determined by NMR spectroscopy
    • Li W., and Hoffman D.W. Structure and dynamics of translation initiation factor aIF-1A from the archaeon Methanococcus jannaschii determined by NMR spectroscopy. Protein Sci. 10 (2001) 2426-2438
    • (2001) Protein Sci. , vol.10 , pp. 2426-2438
    • Li, W.1    Hoffman, D.W.2
  • 61
    • 25644436944 scopus 로고    scopus 로고
    • Translation initiation: Structures, mechanisms and evolution
    • Marintchev A., and Wagner G. Translation initiation: Structures, mechanisms and evolution. Q. Rev. Biophys. 37 (2004) 197-284
    • (2004) Q. Rev. Biophys. , vol.37 , pp. 197-284
    • Marintchev, A.1    Wagner, G.2
  • 64
    • 0033610476 scopus 로고    scopus 로고
    • Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes
    • Matsuo H., Walters K.J., Teruya K., Tanaka T., Gassner G.T., Lippard S.J., Kyogoku Y., and Wagner G. Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes. J. Am. Chem. Soc. 121 (1999) 9903-9904
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9903-9904
    • Matsuo, H.1    Walters, K.J.2    Teruya, K.3    Tanaka, T.4    Gassner, G.T.5    Lippard, S.J.6    Kyogoku, Y.7    Wagner, G.8
  • 66
    • 0031566955 scopus 로고    scopus 로고
    • Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution
    • Moreau M., de Cock E., Fortier P.L., Garcia C., Albaret C., Blanquet S., Lallemand J.Y., and Dardel F. Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. J. Mol. Biol. 266 (1997) 15-22
    • (1997) J. Mol. Biol. , vol.266 , pp. 15-22
    • Moreau, M.1    de Cock, E.2    Fortier, P.L.3    Garcia, C.4    Albaret, C.5    Blanquet, S.6    Lallemand, J.Y.7    Dardel, F.8
  • 67
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • Muralidharan V., and Muir T.W. Protein ligation: An enabling technology for the biophysical analysis of proteins. Nat. Methods 3 (2006) 429-438
    • (2006) Nat. Methods , vol.3 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 68
    • 0036302354 scopus 로고    scopus 로고
    • Determination of the interface of a large protein complex by transferred cross-saturation measurements
    • Nakanishi T., Miyazawa M., Sakakura M., Terasawa H., Takahashi H., and Shimada I. Determination of the interface of a large protein complex by transferred cross-saturation measurements. J. Mol. Biol. 318 (2002) 245-259
    • (2002) J. Mol. Biol. , vol.318 , pp. 245-259
    • Nakanishi, T.1    Miyazawa, M.2    Sakakura, M.3    Terasawa, H.4    Takahashi, H.5    Shimada, I.6
  • 69
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger M., Delaglio F., and Bax A. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 131 (1998) 373-378
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 70
    • 0034984208 scopus 로고    scopus 로고
    • Nmr probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer III A.G. Nmr probes of molecular dynamics: Overview and comparison with other techniques. Annu. Rev. Biophys. Biomol. Struct. 30 (2001) 129-155
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 129-155
    • Palmer III, A.G.1
  • 71
    • 16244365477 scopus 로고    scopus 로고
    • Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems
    • Palmer III A.G., Grey M.J., and Wang C. Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems. Methods Enzymol. 394 (2005) 430-465
    • (2005) Methods Enzymol. , vol.394 , pp. 430-465
    • Palmer III, A.G.1    Grey, M.J.2    Wang, C.3
  • 72
    • 0035958666 scopus 로고    scopus 로고
    • Solution structure of the catalytic domain of gamma delta resolvase. Implications for the mechanism of catalysis
    • Pan B., Maciejewski M.W., Marintchev A., and Mullen G.P. Solution structure of the catalytic domain of gamma delta resolvase. Implications for the mechanism of catalysis. J. Mol. Biol. 310 (2001) 1089-1107
    • (2001) J. Mol. Biol. , vol.310 , pp. 1089-1107
    • Pan, B.1    Maciejewski, M.W.2    Marintchev, A.3    Mullen, G.P.4
  • 74
    • 25144456011 scopus 로고    scopus 로고
    • Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions
    • Pellecchia M. Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions. Chem. Biol. 12 (2005) 961-971
    • (2005) Chem. Biol. , vol.12 , pp. 961-971
    • Pellecchia, M.1
  • 75
    • 0037325758 scopus 로고    scopus 로고
    • A new strategy for backbone resonance assignment in large proteins using a MQ-HACACO experiment
    • Pervushin K., and Eletsky A. A new strategy for backbone resonance assignment in large proteins using a MQ-HACACO experiment. J. Biomol. NMR 25 (2003) 147-152
    • (2003) J. Biomol. NMR , vol.25 , pp. 147-152
    • Pervushin, K.1    Eletsky, A.2
  • 76
    • 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. 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 (1997) 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
  • 77
    • 33644539839 scopus 로고    scopus 로고
    • NMR distinction of single- and multiple-mode binding of small-molecule protein ligands
    • Reibarkh M., Malia T.J., and Wagner G. NMR distinction of single- and multiple-mode binding of small-molecule protein ligands. J. Am. Chem. Soc. 128 (2006) 2160-2161
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2160-2161
    • Reibarkh, M.1    Malia, T.J.2    Wagner, G.3
  • 78
    • 0031000510 scopus 로고    scopus 로고
    • Direct measurement of angles between bond vectors in high-resolution NMR
    • Reif B., Hennig M., and Griesinger C. Direct measurement of angles between bond vectors in high-resolution NMR. Science 276 (1997) 1230-1233
    • (1997) Science , vol.276 , pp. 1230-1233
    • Reif, B.1    Hennig, M.2    Griesinger, C.3
  • 79
    • 4243138246 scopus 로고    scopus 로고
    • Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction
    • Rovnyak D., Frueh D.P., Sastry M., Sun Z.Y., Stern A.S., Hoch J.C., and Wagner G. Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction. J. Magn. Reson. 170 (2004) 15-21
    • (2004) J. Magn. Reson. , vol.170 , pp. 15-21
    • Rovnyak, D.1    Frueh, D.P.2    Sastry, M.3    Sun, Z.Y.4    Stern, A.S.5    Hoch, J.C.6    Wagner, G.7
  • 80
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
    • Salzmann M., Pervushin K., Wider G., Senn H., and Wuthrich K. TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins. Proc. Natl. Acad. Sci. USA 95 (1998) 13585-13590
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wuthrich, K.5
  • 81
    • 0002522872 scopus 로고
    • A simultaneous 15N.1H and 13C,1H-HSQC with sensitivity enhancement and a heteronuclear gradient echo
    • Sattler M., Maurer M., Schleucher J., and Griesinger C. A simultaneous 15N.1H and 13C,1H-HSQC with sensitivity enhancement and a heteronuclear gradient echo. J. Biomol. NMR 5 (1995) 97-102
    • (1995) J. Biomol. NMR , vol.5 , pp. 97-102
    • Sattler, M.1    Maurer, M.2    Schleucher, J.3    Griesinger, C.4
  • 82
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M., Schleucher J., and Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Progr. NMR Spectrosc. 34 (1999) 93-158
    • (1999) Progr. NMR Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 83
    • 0027661526 scopus 로고
    • Application of nonlinear sampling schemes to COSY-type spectra
    • Schmieder P., Stern A.S., Wagner G., and Hoch J.C. Application of nonlinear sampling schemes to COSY-type spectra. J. Biomol. NMR 3 (1993) 569-576
    • (1993) J. Biomol. NMR , vol.3 , pp. 569-576
    • Schmieder, P.1    Stern, A.S.2    Wagner, G.3    Hoch, J.C.4
  • 85
    • 0031002350 scopus 로고    scopus 로고
    • The structure of the translational initiation factor IF1 from E. coli contains an oligomer-binding motif
    • Sette M., van Tilborg P., Spurio R., Kaptein R., Paci M., Gualerzi C.O., and Boelens R. The structure of the translational initiation factor IF1 from E. coli contains an oligomer-binding motif. EMBO J. 16 (1997) 1436-1443
    • (1997) EMBO J. , vol.16 , pp. 1436-1443
    • Sette, M.1    van Tilborg, P.2    Spurio, R.3    Kaptein, R.4    Paci, M.5    Gualerzi, C.O.6    Boelens, R.7
  • 86
    • 16244366419 scopus 로고    scopus 로고
    • NMR techniques for identifying the interface of a larger protein-protein complex: Cross-saturation and transferred cross-saturation experiments
    • Shimada I. NMR techniques for identifying the interface of a larger protein-protein complex: Cross-saturation and transferred cross-saturation experiments. Methods Enzymol. 394 (2005) 483-506
    • (2005) Methods Enzymol. , vol.394 , pp. 483-506
    • Shimada, I.1
  • 87
    • 0042011171 scopus 로고    scopus 로고
    • Solution structure of the C-terminal domain from poly(A)-binding protein in Trypanosoma cruzi: A vegetal PABC domain
    • Siddiqui N., Kozlov G., D'Orso I., Trempe J.F., and Gehring K. Solution structure of the C-terminal domain from poly(A)-binding protein in Trypanosoma cruzi: A vegetal PABC domain. Protein Sci. 12 (2003) 1925-1933
    • (2003) Protein Sci. , vol.12 , pp. 1925-1933
    • Siddiqui, N.1    Kozlov, G.2    D'Orso, I.3    Trempe, J.F.4    Gehring, K.5
  • 88
    • 27644462754 scopus 로고    scopus 로고
    • Fast assignment of (15)N-HSQC peaks using high-resolution 3D HNcocaNH experiments with non-uniform sampling
    • Sun Z.Y., Frueh D.P., Selenko P., Hoch J.C., and Wagner G. Fast assignment of (15)N-HSQC peaks using high-resolution 3D HNcocaNH experiments with non-uniform sampling. J. Biomol. NMR 33 (2005) 43-50
    • (2005) J. Biomol. NMR , vol.33 , pp. 43-50
    • Sun, Z.Y.1    Frueh, D.P.2    Selenko, P.3    Hoch, J.C.4    Wagner, G.5
  • 89
    • 23144464546 scopus 로고    scopus 로고
    • High-resolution aliphatic side-chain assignments in 3D HCcoNH experiments with joint H-C evolution and non-uniform sampling
    • Sun Z.Y., Hyberts S.G., Rovnyak D., Park S., Stern A.S., Hoch J.C., and Wagner G. High-resolution aliphatic side-chain assignments in 3D HCcoNH experiments with joint H-C evolution and non-uniform sampling. J. Biomol. NMR 32 (2005) 55-60
    • (2005) J. Biomol. NMR , vol.32 , pp. 55-60
    • Sun, Z.Y.1    Hyberts, S.G.2    Rovnyak, D.3    Park, S.4    Stern, A.S.5    Hoch, J.C.6    Wagner, G.7
  • 90
    • 33645785076 scopus 로고    scopus 로고
    • Utilization of methyl proton resonances in cross-saturation measurement for determining the interfaces of large protein-protein complexes
    • Takahashi H., Miyazawa M., Ina Y., Fukunishi Y., Mizukoshi Y., Nakamura H., and Shimada I. Utilization of methyl proton resonances in cross-saturation measurement for determining the interfaces of large protein-protein complexes. J. Biomol. NMR 34 (2006) 167-177
    • (2006) J. Biomol. NMR , vol.34 , pp. 167-177
    • Takahashi, H.1    Miyazawa, M.2    Ina, Y.3    Fukunishi, Y.4    Mizukoshi, Y.5    Nakamura, H.6    Shimada, I.7
  • 91
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large protein-protein complexes
    • Takahashi H., Nakanishi T., Kami K., Arata Y., and Shimada I. A novel NMR method for determining the interfaces of large protein-protein complexes. Nat. Struct. Biol. 7 (2000) 220-223
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 92
    • 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. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278 (1997) 1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 93
    • 0037048594 scopus 로고    scopus 로고
    • A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy
    • Tolman J.R. A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy. J. Am. Chem. Soc. 124 (2002) 12020-12030
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12020-12030
    • Tolman, J.R.1
  • 94
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
    • Tolman J.R., Flanagan J.M., Kennedy M.A., and Prestegard J.H. Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution. Proc. Natl. Acad. Sci. USA 92 (1995) 9279-9283
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9279-9283
    • Tolman, J.R.1    Flanagan, J.M.2    Kennedy, M.A.3    Prestegard, J.H.4
  • 95
    • 3943074512 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins
    • Tugarinov V., Hwang P.M., and Kay L.E. Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annu. Rev. Biochem. 73 (2004) 107-146
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 107-146
    • Tugarinov, V.1    Hwang, P.M.2    Kay, L.E.3
  • 96
    • 24744447629 scopus 로고    scopus 로고
    • Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins
    • Tugarinov V., and Kay L.E. Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins. Chembiochem 6 (2005) 1567-1577
    • (2005) Chembiochem , vol.6 , pp. 1567-1577
    • Tugarinov, V.1    Kay, L.E.2
  • 97
    • 14744278812 scopus 로고    scopus 로고
    • High-resolution four-dimensional 1H-13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition
    • Tugarinov V., Kay L.E., Ibraghimov I., and Orekhov V.Y. High-resolution four-dimensional 1H-13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition. J. Am. Chem. Soc. 127 (2005) 2767-2775
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2767-2775
    • Tugarinov, V.1    Kay, L.E.2    Ibraghimov, I.3    Orekhov, V.Y.4
  • 99
    • 29544446689 scopus 로고    scopus 로고
    • Weak protein-protein interactions as probed by NMR spectroscopy
    • Vaynberg J., and Qin J. Weak protein-protein interactions as probed by NMR spectroscopy. Trends Biotechnol. 24 (2006) 22-27
    • (2006) Trends Biotechnol. , vol.24 , pp. 22-27
    • Vaynberg, J.1    Qin, J.2
  • 100
    • 0036428702 scopus 로고    scopus 로고
    • Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function
    • von der Haar T., and McCarthy J.E. Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function. Mol. Microbiol. 46 (2002) 531-544
    • (2002) Mol. Microbiol. , vol.46 , pp. 531-544
    • von der Haar, T.1    McCarthy, J.E.2
  • 102
    • 0001050734 scopus 로고    scopus 로고
    • A simple method to distinguish intermonomer nuclear Overhauser effects in homodimeric proteins with C2 symmetry
    • Walters K.J., Matsuo H., and Wagner G. A simple method to distinguish intermonomer nuclear Overhauser effects in homodimeric proteins with C2 symmetry. J. Am. Chem. Soc. 119 (1997) 5958-5959
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5958-5959
    • Walters, K.J.1    Matsuo, H.2    Wagner, G.3
  • 105
    • 0027357769 scopus 로고
    • 3D triple-resonance NMR techniques for the sequential assignment of NH and 15N resonances in 15N- and 13C-labelled proteins
    • Weisemann R., Ruterjans H., and Bermel W. 3D triple-resonance NMR techniques for the sequential assignment of NH and 15N resonances in 15N- and 13C-labelled proteins. J. Biomol. NMR 3 (1993) 113-120
    • (1993) J. Biomol. NMR , vol.3 , pp. 113-120
    • Weisemann, R.1    Ruterjans, H.2    Bermel, W.3
  • 106
    • 24344440731 scopus 로고    scopus 로고
    • Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2
    • Wienk H., Tomaselli S., Bernard C., Spurio R., Picone D., Gualerzi C.O., and Boelens R. Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2. Protein Sci. 14 (2005) 2461-2468
    • (2005) Protein Sci. , vol.14 , pp. 2461-2468
    • Wienk, H.1    Tomaselli, S.2    Bernard, C.3    Spurio, R.4    Picone, D.5    Gualerzi, C.O.6    Boelens, R.7
  • 107
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • Wittekind M., and Mueller L. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. JMRB 101 (1993) 201-205
    • (1993) JMRB , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 108
    • 0035040149 scopus 로고    scopus 로고
    • 3D Haro-NOESY-CH3NH and Caro-NOESY-CH3NH experiments for double labeled proteins
    • Xia Y., and Zhu G. 3D Haro-NOESY-CH3NH and Caro-NOESY-CH3NH experiments for double labeled proteins. J. Biomol. NMR 19 (2001) 355-360
    • (2001) J. Biomol. NMR , vol.19 , pp. 355-360
    • Xia, Y.1    Zhu, G.2
  • 109
    • 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. A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins. J. Biomol. NMR 20 (2001) 11-14
    • (2001) J. Biomol. NMR , vol.20 , pp. 11-14
    • Zhou, P.1    Lugovskoy, A.A.2    Wagner, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.