메뉴 건너뛰기




Volumn 323, Issue 3, 2002, Pages 463-473

TROSY-NMR studies of the 91 kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility

Author keywords

Allostery; Dynamics; TRAP; TROSY; Tryptophan

Indexed keywords

BACTERIAL PROTEIN; ISOPROTEIN; REGULATOR PROTEIN; RNA; TRYPTOPHAN; TRYPTOPHAN RNA BINDING ATTENUATION PROTEIN; UNCLASSIFIED DRUG;

EID: 0036416144     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00940-3     Document Type: Article
Times cited : (68)

References (49)
  • 1
    • 0024041531 scopus 로고
    • Cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon
    • Kuroda, M. I., Henner, D. & Yanofsky, C. (1988). Cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon. J. Bacteriol. 170, 3080-3088.
    • (1988) J. Bacteriol. , vol.170 , pp. 3080-3088
    • Kuroda, M.I.1    Henner, D.2    Yanofsky, C.3
  • 2
    • 0028906665 scopus 로고
    • The mtrB gene of Bacillus pumilus encodes a protein with sequence and functional homology to the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis
    • Hoffman, R. J. & Gollnick, P. (1995). The mtrB gene of Bacillus pumilus encodes a protein with sequence and functional homology to the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis. J. Bacteriol. 177, 839-842.
    • (1995) J. Bacteriol. , vol.177 , pp. 839-842
    • Hoffman, R.J.1    Gollnick, P.2
  • 3
    • 0028217753 scopus 로고
    • Regulation of the Bacillus subtilis trp operon by an RNA-binding protein
    • Gollnick, P. (1994). Regulation of the Bacillus subtilis trp operon by an RNA-binding protein. Mol. Microbiol. 11, 991-997.
    • (1994) Mol. Microbiol. , vol.11 , pp. 991-997
    • Gollnick, P.1
  • 4
    • 0030821725 scopus 로고    scopus 로고
    • Regulation of tryptophan biosynthesis: Trp-ing the TRAP or how Bacillus subtilis reinvented the wheel
    • Babitzke, P. (1997). Regulation of tryptophan biosynthesis: Trp-ing the TRAP or how Bacillus subtilis reinvented the wheel. Mol. Microbiol. 26, 1-9.
    • (1997) Mol. Microbiol. , vol.26 , pp. 1-9
    • Babitzke, P.1
  • 5
    • 0033022150 scopus 로고    scopus 로고
    • Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus
    • Chen, X., Antson, A. A., Yang, M., Li, P., Baumann, C., Dodson, E. J. et al. (1999). Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus. J. Mol. Biol. 289, 1003-1016.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1003-1016
    • Chen, X.1    Antson, A.A.2    Yang, M.3    Li, P.4    Baumann, C.5    Dodson, E.J.6
  • 6
    • 0027509047 scopus 로고
    • MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner
    • Otridge, J. & Gollnick, P. (1993). MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner. Proc. Natl. Acad. Sci. USA, 90, 128-132.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 128-132
    • Otridge, J.1    Gollnick, P.2
  • 8
    • 0033575897 scopus 로고    scopus 로고
    • Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
    • Antson, A. A., Dodson, E. J., Dodson, G., Greaves, R. B., Chen, X. & Gollnick, P. (1999). Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA. Nature, 401, 235-242.
    • (1999) Nature , vol.401 , pp. 235-242
    • Antson, A.A.1    Dodson, E.J.2    Dodson, G.3    Greaves, R.B.4    Chen, X.5    Gollnick, P.6
  • 9
    • 0035179356 scopus 로고    scopus 로고
    • Crystal structure of transcription factor MalT domain III: A novel helix repeat fold implicated in regulated oligomerization
    • Steegborn, C., Danot, O., Huber, R. & Clausen, T. (2001). Crystal structure of transcription factor MalT domain III: A novel helix repeat fold implicated in regulated oligomerization. Structure, 9, 1051-1060.
    • (2001) Structure , vol.9 , pp. 1051-1060
    • Steegborn, C.1    Danot, O.2    Huber, R.3    Clausen, T.4
  • 10
    • 0033585068 scopus 로고    scopus 로고
    • Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP
    • Schreiber, V. & Richet, E. (1999). Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP. J. Biol. Chem. 274, 33220-33226.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33220-33226
    • Schreiber, V.1    Richet, E.2
  • 11
    • 0035852714 scopus 로고    scopus 로고
    • The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization
    • Zhu, J. & Winans, S. C. (2001). The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization. Proc. Natl. Acad. Sci. USA, 98, 1507-1512.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1507-1512
    • Zhu, J.1    Winans, S.C.2
  • 12
    • 0037182879 scopus 로고    scopus 로고
    • Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA
    • Zhang, R. G., Pappas, T., Brace, J. L., Miller, P. C., Oulmassov, T., Molyneaux, J. M. et al. (2002). Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA. Nature, 417, 971-974.
    • (2002) Nature , vol.417 , pp. 971-974
    • Zhang, R.G.1    Pappas, T.2    Brace, J.L.3    Miller, P.C.4    Oulmassov, T.5    Molyneaux, J.M.6
  • 13
    • 0035937734 scopus 로고    scopus 로고
    • Control of retinoic acid receptor heterodimerization by ligand-induced structural transitions. A novel mechanism of action for retinoid antagonists
    • Depoix, C., Delmotte, M. H., Formstecher, P. & Lefebvre, P. (2001). Control of retinoic acid receptor heterodimerization by ligand-induced structural transitions. A novel mechanism of action for retinoid antagonists. J. Biol. Chem. 276, 9452-9459.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9452-9459
    • Depoix, C.1    Delmotte, M.H.2    Formstecher, P.3    Lefebvre, P.4
  • 14
    • 0037023767 scopus 로고    scopus 로고
    • Creating hetero-11-mers composed of wild-type and mutant subunits to study RNA binding to TRAP
    • Li, P. T., Scott, D. & Gollnick, P. (2002). Creating hetero-11-mers composed of wild-type and mutant subunits to study RNA binding to TRAP. J. Biol. Chem. 227, 11838-11844.
    • (2002) J. Biol. Chem. , vol.227 , pp. 11838-11844
    • Li, P.T.1    Scott, D.2    Gollnick, P.3
  • 15
    • 0034671172 scopus 로고    scopus 로고
    • Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 Å resolution
    • Passner, J. M., Schultz, S. C. & Steitz, T. A. (2000). Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 Å resolution. J. Mol. Biol. 304, 847-859.
    • (2000) J. Mol. Biol. , vol.304 , pp. 847-859
    • Passner, J.M.1    Schultz, S.C.2    Steitz, T.A.3
  • 17
    • 0025797334 scopus 로고
    • Characterization of DNA binding and retinoic acid binding properties of retinoic acid receptor
    • Yang, N., Schule, R., Mangelsdorf, D. J. & Evans, R. M. (1991). Characterization of DNA binding and retinoic acid binding properties of retinoic acid receptor. Proc. Natl. Acad. Sci. USA, 88, 3559-3563.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3559-3563
    • Yang, N.1    Schule, R.2    Mangelsdorf, D.J.3    Evans, R.M.4
  • 18
    • 0034213831 scopus 로고    scopus 로고
    • Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid
    • Egea, P. F., Mitschler, A., Rochel, N., Ruff, M., Chambon, P. & Moras, D. (2000). Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. EMBO J. 19, 2592-2601.
    • (2000) EMBO J. , vol.19 , pp. 2592-2601
    • Egea, P.F.1    Mitschler, A.2    Rochel, N.3    Ruff, M.4    Chambon, P.5    Moras, D.6
  • 19
    • 0036182617 scopus 로고    scopus 로고
    • A residue-specific view of the association and dissociation pathway in protein-DNA recognition
    • Kalodimos, C. G., Boelens, R. & Kaptein, R. (2002). A residue-specific view of the association and dissociation pathway in protein-DNA recognition. Nature Struct. Biol. 9, 193-197.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 193-197
    • Kalodimos, C.G.1    Boelens, R.2    Kaptein, R.3
  • 20
    • 0001098977 scopus 로고
    • Unusual dynamic features of the trp repressor from Escherichia coli
    • Arrowsmith, C. H., Czaplicki, J., Iyer, S. B. & Jardetzky, O. (1991). Unusual dynamic features of the trp repressor from Escherichia coli. J. Am. Chem. Soc. 113, 4020-4022.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4020-4022
    • Arrowsmith, C.H.1    Czaplicki, J.2    Iyer, S.B.3    Jardetzky, O.4
  • 21
    • 0026015213 scopus 로고
    • The solution structures of Escherichia coli trp repressor and trp aporepressor at an intermediate resolution
    • Arrowsmith, C., Pachter, R., Altman, R. & Jardetzky, O. (1991). The solution structures of Escherichia coli trp repressor and trp aporepressor at an intermediate resolution. Eur. J. Biochem. 202, 53-66.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 53-66
    • Arrowsmith, C.1    Pachter, R.2    Altman, R.3    Jardetzky, O.4
  • 22
    • 0027528411 scopus 로고
    • Refined solution structures of the Escherichia coli trp holo- and aporepressor
    • Zhao, D., Arrowsmith, C. H., Jia, X. & Jardetzky, O. (1993). Refined solution structures of the Escherichia coli trp holo- and aporepressor. J. Mol. Biol. 229, 735-746.
    • (1993) J. Mol. Biol. , vol.229 , pp. 735-746
    • Zhao, D.1    Arrowsmith, C.H.2    Jia, X.3    Jardetzky, O.4
  • 23
    • 0034254326 scopus 로고    scopus 로고
    • Changes in dynamical behavior of the retinoid X receptor DNA-binding domain upon binding to a 14 base-pair DNA half site
    • van Tilborg, P. J., Czisch, M., Mulder, F. A., Folkers, G. E., Bonvin, A. M., Nair, M. et al. (2000). Changes in dynamical behavior of the retinoid X receptor DNA-binding domain upon binding to a 14 base-pair DNA half site. Biochemistry, 39, 8747-8757.
    • (2000) Biochemistry , vol.39 , pp. 8747-8757
    • Van Tilborg, P.J.1    Czisch, M.2    Mulder, F.A.3    Folkers, G.E.4    Bonvin, A.M.5    Nair, M.6
  • 24
    • 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. & 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
  • 25
    • 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. & Wuthrich, K. (1998). TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins. Proc. Natl. Acad. Sci. USA, 95, 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
  • 28
    • 0032622242 scopus 로고    scopus 로고
    • Sensitivity improvement of transverse relaxation-optimized spectroscopy
    • Rance, M., Loria, J. P. & Palmer, A. G. r. (1999). Sensitivity improvement of transverse relaxation-optimized spectroscopy. J. Magn. Reson. 136, 92-101.
    • (1999) J. Magn. Reson. , vol.136 , pp. 92-101
    • Rance, M.1    Loria, J.P.2    Palmer, A.G.R.3
  • 29
    • 0033226859 scopus 로고    scopus 로고
    • Transverse-relaxation-optimized (TROSY) gradient-enhanced triple-resonance NMR spectroscopy
    • Loria, J. P., Rance, M. & Palmer, A. G., III (1999). Transverse-relaxation-optimized (TROSY) gradient-enhanced triple-resonance NMR spectroscopy. J. Magn. Reson. 141, 180-184.
    • (1999) J. Magn. Reson. , vol.141 , pp. 180-184
    • Loria, J.P.1    Rance, M.2    Palmer A.G. III3
  • 30
    • 0029997474 scopus 로고    scopus 로고
    • 1H-NMR characterization of L-tryptophan binding to TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis
    • Ramesh, V. & Brown, T. (1996). 1H-NMR characterization of L-tryptophan binding to TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis. Biochem. J. 315, 895-900.
    • (1996) Biochem. J. , vol.315 , pp. 895-900
    • Ramesh, V.1    Brown, T.2
  • 31
    • 0031214216 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding
    • Yang, M., Chen, X., Militello, K., Hoffman, R., Fernandez, B., Baumann, C. & Gollnick, P. (1997). Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding. J. Mol. Biol. 270, 696-710.
    • (1997) J. Mol. Biol. , vol.270 , pp. 696-710
    • Yang, M.1    Chen, X.2    Militello, K.3    Hoffman, R.4    Fernandez, B.5    Baumann, C.6    Gollnick, P.7
  • 32
    • 17544365656 scopus 로고    scopus 로고
    • Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA
    • Baumann, C., Otridge, J. & Gollnick, P. (1996). Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA. J. Biol. Chem. 271, 12269-12274.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12269-12274
    • Baumann, C.1    Otridge, J.2    Gollnick, P.3
  • 33
    • 0029938053 scopus 로고    scopus 로고
    • Crystal structure of the lactose operon repressor and its complexes with DNA and inducer
    • Lewis, M., Chang, G., Horton, N. C., Kercher, M. A., Pace, H. C., Schumacher, M. A. et al. (1996). Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Science, 271, 1247-1254.
    • (1996) Science , vol.271 , pp. 1247-1254
    • Lewis, M.1    Chang, G.2    Horton, N.C.3    Kercher, M.A.4    Pace, H.C.5    Schumacher, M.A.6
  • 34
    • 0035253082 scopus 로고    scopus 로고
    • The Lac repressor: A second generation of structural and functional studies
    • Bell, C. E. & Lewis, M. (2001). The Lac repressor: A second generation of structural and functional studies. Curr. Opin. Struct. Biol. 11, 19-25.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 19-25
    • Bell, C.E.1    Lewis, M.2
  • 35
    • 0034089394 scopus 로고    scopus 로고
    • A closer view of the conformation of the Lac repressor bound to operator
    • Bell, C. E. & Lewis, M. (2000). A closer view of the conformation of the Lac repressor bound to operator. Nature Struct. Biol. 7, 209-214.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 209-214
    • Bell, C.E.1    Lewis, M.2
  • 36
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • Perutz, M. F. (1989). Mechanisms of cooperativity and allosteric regulation in proteins. Quart. Rev. Biophys. 22, 139-237.
    • (1989) Quart. Rev. Biophys. , vol.22 , pp. 139-237
    • Perutz, M.F.1
  • 37
    • 0030433170 scopus 로고    scopus 로고
    • Protein dynamics and conformational transitions in allosteric proteins
    • Jardetzky, O. (1996). Protein dynamics and conformational transitions in allosteric proteins. Prog. Biophys. Mol. Biol. 65, 171-219.
    • (1996) Prog. Biophys. Mol. Biol. , vol.65 , pp. 171-219
    • Jardetzky, O.1
  • 38
    • 0033642945 scopus 로고    scopus 로고
    • Structural stability of binding sites: Consequences for binding affinity and allosteric effects
    • Luque, I. & Freire, E. (2000). Structural stability of binding sites: Consequences for binding affinity and allosteric effects. Proteins: Struct. Funct. Genet., 63-71.
    • (2000) Proteins: Struct. Funct. Genet. , pp. 63-71
    • Luque, I.1    Freire, E.2
  • 39
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant, J. M. (1977). Heat capacity and entropy changes in processes involving proteins. Proc. Natl. Acad. Sci. USA, 74, 2236-2240.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 40
    • 0021658956 scopus 로고
    • Allostery without conformational change. A plausible model
    • Cooper, A. & Dryden, D. T. (1984). Allostery without conformational change. A plausible model. Eur. Biophys. J. 11, 103-109.
    • (1984) Eur. Biophys. J , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.2
  • 41
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S. & Record, M. T., Jr (1994). Coupling of local folding to site-specific binding of proteins to DNA. Science, 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record M.T., Jr.2
  • 42
    • 0033784534 scopus 로고    scopus 로고
    • Induced fit in RNA-protein recognition
    • Williamson, J. R. (2000). Induced fit in RNA-protein recognition. Nature Struct. Biol. 7, 834-837.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 834-837
    • Williamson, J.R.1
  • 43
    • 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. & Griesinger, C. (1999). Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. NMR Spectrosc. 34, 93-158.
    • (1999) Prog. NMR Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 44
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & 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
  • 45
    • 34249765651 scopus 로고
    • NMR View - A computer-program for the visualization and analysis of NMR data
    • Johnson, B. & Blevins, R. (1994). NMR View - A computer-program for the visualization and analysis of NMR data. J. Biomol. NMR, 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.1    Blevins, R.2
  • 46
    • 0032113850 scopus 로고    scopus 로고
    • Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA
    • Foster, M. P., Wuttke, D. S., Clemens, K. R., Jahnke, W., Radhakrishnan, I., Tennant, L. et al. (1998). Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA. J. Biomol. NMR, 12, 51-71.
    • (1998) J. Biomol. NMR , vol.12 , pp. 51-71
    • Foster, M.P.1    Wuttke, D.S.2    Clemens, K.R.3    Jahnke, W.4    Radhakrishnan, I.5    Tennant, L.6
  • 47
    • 0030936560 scopus 로고    scopus 로고
    • Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phospho-transferase system
    • Garrett, D. S., Seok, Y. J., Peterkofsky, A., Clore, G. M. & Gronenborn, A. M. (1997). Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phospho-transferase system. Biochemistry, 36, 4393-4398.
    • (1997) Biochemistry , vol.36 , pp. 4393-4398
    • Garrett, D.S.1    Seok, Y.J.2    Peterkofsky, A.3    Clore, G.M.4    Gronenborn, A.M.5
  • 48
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • Grzesiek, S., Bax, A., Clore, G. M., Gronenborn, A. M., Hu, J. S., Kaufman, J. et al. (1996). The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nature Struct. Biol. 3, 340-345.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4    Hu, J.S.5    Kaufman, J.6
  • 49
    • 0002178305 scopus 로고    scopus 로고
    • MOL-MOL: A program for display and analysis of macro-molecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. (1996). MOL-MOL: A program for display and analysis of macro-molecular structures. J. Mol. Graph. 51-55, 29-32.
    • (1996) J. Mol. Graph. , vol.51-55 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.