메뉴 건너뛰기




Volumn 334, Issue 5, 2003, Pages 901-918

Naturally-occurring Modification Restricts the Anticodon Domain Conformational Space of tRNAPhe

Author keywords

Anticodon dynamics; Codon recognition; Frameshifting; Methylation; tRNA position 37

Indexed keywords

TRANSFER RNA;

EID: 0345304724     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.058     Document Type: Article
Times cited : (69)

References (94)
  • 3
    • 0032870204 scopus 로고    scopus 로고
    • Structural motifs in RNA
    • Moore P.B. Structural motifs in RNA. Annu. Rev. Biochem. 68:1999;287-300.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 287-300
    • Moore, P.B.1
  • 6
    • 0032526960 scopus 로고    scopus 로고
    • The structure of a methylated tetraloop in 16 S ribosomal RNA
    • Rife J.P., Moore P.B. The structure of a methylated tetraloop in 16 S ribosomal RNA. Structure. 6:1998;747-756.
    • (1998) Structure , vol.6 , pp. 747-756
    • Rife, J.P.1    Moore, P.B.2
  • 7
    • 0039547877 scopus 로고
    • A Model Nucleic Acid System for NMR Investigations of Functionally Important Conformational Changes: The tRNA Anticodon
    • J.N. Abelson, & M.I. Simon. Orlando, FL: Academic Press
    • Agris P.F., Brown S.C. A Model Nucleic Acid System for NMR Investigations of Functionally Important Conformational Changes: the tRNA Anticodon. Abelson J.N., Simon M.I. Methods Enzymol. Methods Enzymol. vol. 261:1995;277 Academic Press, Orlando, FL.
    • (1995) Methods Enzymol. , vol.261 , pp. 277
    • Agris, P.F.1    Brown, S.C.2
  • 10
    • 0001918945 scopus 로고    scopus 로고
    • Location and distribution of modified nucleosides in tRNA
    • H. Grosjean, & R. Benne. Washington, DC: American Society for Microbiology Press
    • Aufinger P., Westoff E. Location and distribution of modified nucleosides in tRNA. Grosjean H., Benne R. Modification and Editing of RNA. 1998;569 American Society for Microbiology Press, Washington, DC.
    • (1998) Modification and Editing of RNA , pp. 569
    • Aufinger, P.1    Westoff, E.2
  • 14
  • 15
    • 0034680364 scopus 로고    scopus 로고
    • Hypermodified nucleosides in the anticodon of tRNA(Lys) stabilize a canonical U-turn structure
    • Sundaram M., Durant P.C., Davis D.R. Hypermodified nucleosides in the anticodon of tRNA(Lys) stabilize a canonical U-turn structure. Biochemistry. 39:2000;12575-12584.
    • (2000) Biochemistry , vol.39 , pp. 12575-12584
    • Sundaram, M.1    Durant, P.C.2    Davis, D.R.3
  • 20
    • 0035801515 scopus 로고    scopus 로고
    • Improvement of reading frame maintenance is a common function for several tRNA modifications
    • Urbonavičius J., Qian Q., Durand J.M.B., Hagervall T.G., Björk G.R. Improvement of reading frame maintenance is a common function for several tRNA modifications. EMBO J. 20:2001;4863-4873.
    • (2001) EMBO J. , vol.20 , pp. 4863-4873
    • Urbonavičius, J.1    Qian, Q.2    Durand, J.M.B.3    Hagervall, T.G.4    Björk, G.R.5
  • 21
    • 0035890653 scopus 로고    scopus 로고
    • Post-transcriptional modification in archaeal tRNAs: Identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic Methanococcales
    • McCloskey J.A., Graham D.E., Zhou S., Crain P.F., Ibba M., Konisky J., Söll D., Olsen G.J. Post-transcriptional modification in archaeal tRNAs: identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic Methanococcales. Nucl. Acids Res. 29:2001;4699-4706.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 4699-4706
    • Mccloskey, J.A.1    Graham, D.E.2    Zhou, S.3    Crain, P.F.4    Ibba, M.5    Konisky, J.6    Söll, D.7    Olsen, G.J.8
  • 22
    • 0024316220 scopus 로고
    • Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine
    • Björk G.R., Wikstrom P.M., Bystrom A.S. Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine. Science. 244:1989;986-989.
    • (1989) Science , vol.244 , pp. 986-989
    • Björk, G.R.1    Wikstrom, P.M.2    Bystrom, A.S.3
  • 26
    • 0035916013 scopus 로고    scopus 로고
    • 1-Methylguanosine in place of Y base at position 37 in phenylalanine tRNA is responsible for its shiftiness in retroviral ribosomal frame shifting
    • Carlson B.A., Mushinski J.F., Henderson D.W., Kwon S.Y., Crain P.F., Lee B.J., Hatfield D.L. 1-Methylguanosine in place of Y base at position 37 in phenylalanine tRNA is responsible for its shiftiness in retroviral ribosomal frame shifting. Virology. 279:2001;130-135.
    • (2001) Virology , vol.279 , pp. 130-135
    • Carlson, B.A.1    Mushinski, J.F.2    Henderson, D.W.3    Kwon, S.Y.4    Crain, P.F.5    Lee, B.J.6    Hatfield, D.L.7
  • 30
    • 0028180696 scopus 로고
    • Phe are not essential for ternary complex formation and peptide elongation
    • Phe are not essential for ternary complex formation and peptide elongation. EMBO J. 13:1994;2464-2471.
    • (1994) EMBO J. , vol.13 , pp. 2464-2471
    • Nazarenko, I.A.1    Harrington, K.M.2    Uhlenbeck, O.C.3
  • 33
    • 0035960675 scopus 로고    scopus 로고
    • Phe are significant recognition determinants in the binding of a phage display selected peptide
    • Phe are significant recognition determinants in the binding of a phage display selected peptide. Biochemistry. 40:2001;14191-14199.
    • (2001) Biochemistry , vol.40 , pp. 14191-14199
    • Mucha, P.1    Szyk, A.2    Rekowski, A.3    Weiss, P.A.4    Agris, P.F.5
  • 40
    • 0001628092 scopus 로고
    • Carbon assignments and heteronuclear coupling constants for an RNA oligonucleotide from natural abundance carbon-13-proton correlated experiments
    • Varani G., Tinoco I. Jr. Carbon assignments and heteronuclear coupling constants for an RNA oligonucleotide from natural abundance carbon-13-proton correlated experiments. J. Am. Chem. Soc. 113:1991;9349-9354.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9349-9354
    • Varani, G.1    Tinoco Jr., I.2
  • 41
    • 0028004616 scopus 로고
    • In situ probing of adenine protonation in RNA by 13C NMR
    • Legault P., Pardi A. In situ probing of adenine protonation in RNA by 13C NMR. J. Am. Chem. Soc. 116:1994;8390-8391.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8390-8391
    • Legault, P.1    Pardi, A.2
  • 42
    • 0029869856 scopus 로고    scopus 로고
    • Solution structure of loop a from the hairpin ribozyme from tobacco ringspot virus satellite
    • Cai Z., Tinoco I. Jr. Solution structure of loop a from the hairpin ribozyme from tobacco ringspot virus satellite. Biochemistry. 35:1996;6026-6036.
    • (1996) Biochemistry , vol.35 , pp. 6026-6036
    • Cai, Z.1    Tinoco Jr., I.2
  • 43
    • 0030747007 scopus 로고    scopus 로고
    • a shift at the active site of a lead-dependent ribozyme
    • a shift at the active site of a lead-dependent ribozyme. J. Am. Chem. Soc. 119:1997;6621-6628.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6621-6628
    • Legault, P.1    Pardi, A.2
  • 44
    • 0034719109 scopus 로고    scopus 로고
    • Adenine protonation in domain B of the hairpin ribozyme
    • Ravindranathan S., Butcher S.E., Feigon J. Adenine protonation in domain B of the hairpin ribozyme. Biochemistry. 39:2000;16026-16032.
    • (2000) Biochemistry , vol.39 , pp. 16026-16032
    • Ravindranathan, S.1    Butcher, S.E.2    Feigon, J.3
  • 45
    • 0033049745 scopus 로고    scopus 로고
    • Solution structure of the loop B domain from the hairpin ribozyme
    • Butcher S.E., Alain F.H.-T., Feigon J. Solution structure of the loop B domain from the hairpin ribozyme. Nature Struct. Biol. 6:1999;212-216.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 212-216
    • Butcher, S.E.1    Alain, F.H.-T.2    Feigon, J.3
  • 46
    • 0029998660 scopus 로고    scopus 로고
    • Structure of a hexanucleotide RNA hairpin loop conserved in ribosomal RNAs
    • Huang S., Wang Y.X., Draper D.E. Structure of a hexanucleotide RNA hairpin loop conserved in ribosomal RNAs. J. Mol. Biol. 258:1996;308-321.
    • (1996) J. Mol. Biol. , vol.258 , pp. 308-321
    • Huang, S.1    Wang, Y.X.2    Draper, D.E.3
  • 48
    • 0031552368 scopus 로고    scopus 로고
    • On the conformation of the anticodon loops of initiator and elongator methionine tRNAs
    • Schweisguth D.C., Moore P.B. On the conformation of the anticodon loops of initiator and elongator methionine tRNAs. J. Mol. Biol. 267:1997;505-519.
    • (1997) J. Mol. Biol. , vol.267 , pp. 505-519
    • Schweisguth, D.C.1    Moore, P.B.2
  • 49
    • 0034703758 scopus 로고    scopus 로고
    • A global structure of RNA determined with residual dipolar couplings
    • Mollova E.T., Hansen M.R., Pardi A. A global structure of RNA determined with residual dipolar couplings. J. Am. Chem. Soc. 122:2000;11561-11562.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11561-11562
    • Mollova, E.T.1    Hansen, M.R.2    Pardi, A.3
  • 51
    • 0036786817 scopus 로고    scopus 로고
    • The global conformation of the hammerhead ribozyme determined using residual dipolar couplings
    • Bondensgaard K., Mollova E.T., Pardi A. The global conformation of the hammerhead ribozyme determined using residual dipolar couplings. Biochemistry. 41:2002;11532-11542.
    • (2002) Biochemistry , vol.41 , pp. 11532-11542
    • Bondensgaard, K.1    Mollova, E.T.2    Pardi, A.3
  • 52
    • 0037470595 scopus 로고    scopus 로고
    • Refined solution structure of the iron-responsive element RNA using residual dipolar couplings
    • McCallum S.A., Pardi A. Refined solution structure of the iron-responsive element RNA using residual dipolar couplings. J. Mol. Biol. 326:2003;1037-1050.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1037-1050
    • Mccallum, S.A.1    Pardi, A.2
  • 55
    • 0035928804 scopus 로고    scopus 로고
    • Structural characterization of a six-nucleotide RNA hairpin loop found in Escherichia coli, r(UUAAGU)
    • Zhang H., Fountain M.A., Krugh T.R. Structural characterization of a six-nucleotide RNA hairpin loop found in Escherichia coli, r(UUAAGU). Biochemistry. 40:2001;9879-9886.
    • (2001) Biochemistry , vol.40 , pp. 9879-9886
    • Zhang, H.1    Fountain, M.A.2    Krugh, T.R.3
  • 56
    • 0018121584 scopus 로고
    • Crystal structure of yeast phenylalanine transfer RNA. II. Structural features and functional implications
    • Holbrook S.R., Sussman J.L., Warrant R.W., Kim S.-H. Crystal structure of yeast phenylalanine transfer RNA. II. Structural features and functional implications. J. Mol. Biol. 123:1978;631-660.
    • (1978) J. Mol. Biol. , vol.123 , pp. 631-660
    • Holbrook, S.R.1    Sussman, J.L.2    Warrant, R.W.3    Kim, S.-H.4
  • 57
    • 0025925206 scopus 로고
    • Stabilities of consecutive A·C, C·C, G·G, U·C, and U·U mismatches in RNA internal loops: Evidence for stable hydrogen-bonded U·U and C·C·+pairs
    • SantaLucia J. Jr, Kierzek R., Turner D.H. Stabilities of consecutive A·C, C·C, G·G, U·C, and U·U mismatches in RNA internal loops: evidence for stable hydrogen-bonded U·U and C·C·+pairs. Biochemistry. 30:1991;8242-8251.
    • (1991) Biochemistry , vol.30 , pp. 8242-8251
    • Santalucia Jr., J.1    Kierzek, R.2    Turner, D.H.3
  • 60
    • 0036295962 scopus 로고    scopus 로고
    • A cytosolic tRNA with an unmodified adenosine in the wobble position reads a codon ending with the non-complementary nucleoside cytidine
    • Chen P., Qian Q., Zhang S., Isaksson L.A., Björk G.R. A cytosolic tRNA with an unmodified adenosine in the wobble position reads a codon ending with the non-complementary nucleoside cytidine. J. Mol. Biol. 317:2002;481-492.
    • (2002) J. Mol. Biol. , vol.317 , pp. 481-492
    • Chen, P.1    Qian, Q.2    Zhang, S.3    Isaksson, L.A.4    Björk, G.R.5
  • 61
    • 0014210985 scopus 로고
    • Conformation of the anticodon loop in tRNA
    • Fuller W., Hodgson A. Conformation of the anticodon loop in tRNA. Nature. 215:1967;817-821.
    • (1967) Nature , vol.215 , pp. 817-821
    • Fuller, W.1    Hodgson, A.2
  • 63
    • 0014842780 scopus 로고
    • Studies on the conformation of the anticodon of phenylalanine transfer ribonucleic acid. Effect of environment on the fluorescence of the Y base
    • Beardsley K., Tao T., Cantor C.R. Studies on the conformation of the anticodon of phenylalanine transfer ribonucleic acid. Effect of environment on the fluorescence of the Y base. Biochemistry. 9:1970;3524-3532.
    • (1970) Biochemistry , vol.9 , pp. 3524-3532
    • Beardsley, K.1    Tao, T.2    Cantor, C.R.3
  • 65
  • 67
    • 0036896469 scopus 로고    scopus 로고
    • Sculpting of the spliceosomal branch site recognition motif by a conserved pseudouridine
    • Newby M.I., Greenbaum N.L. Sculpting of the spliceosomal branch site recognition motif by a conserved pseudouridine. Nature Struct. Biol. 9:2002;958-965.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 958-965
    • Newby, M.I.1    Greenbaum, N.L.2
  • 69
    • 0033744175 scopus 로고    scopus 로고
    • The crystal structure of HIV reverse-transcription primer tRNA(Lys,3) shows a canonical anticodon loop
    • Benas P., Bec G., Keith G., Marquet R., Ehresmann C., Ehresmann B., Dumas P. The crystal structure of HIV reverse-transcription primer tRNA(Lys,3) shows a canonical anticodon loop. RNA. 6:2000;1347-1355.
    • (2000) RNA , vol.6 , pp. 1347-1355
    • Benas, P.1    Bec, G.2    Keith, G.3    Marquet, R.4    Ehresmann, C.5    Ehresmann, B.6    Dumas, P.7
  • 71
    • 0017165207 scopus 로고
    • Studies of the complex between transfer RNAs with complementary anticodons I. Origins of enhanced affinity between complementary triplets
    • Grosjean H., Söll D., Crothers D.M. Studies of the complex between transfer RNAs with complementary anticodons I. Origins of enhanced affinity between complementary triplets. J. Mol. Biol. 103:1976;499-519.
    • (1976) J. Mol. Biol. , vol.103 , pp. 499-519
    • Grosjean, H.1    Söll, D.2    Crothers, D.M.3
  • 73
    • 0028915734 scopus 로고
    • Site-selected introduction of modified purine and pyrimidine ribonucleosides into RNA by automated phosphoramidite chemistry
    • Agris P.F., Malkiewicz A., Brown S., Kraszewski A., Nawrot B., Sochacka E., et al. Site-selected introduction of modified purine and pyrimidine ribonucleosides into RNA by automated phosphoramidite chemistry. Biochimie. 77:1995;125-134.
    • (1995) Biochimie , vol.77 , pp. 125-134
    • Agris, P.F.1    Malkiewicz, A.2    Brown, S.3    Kraszewski, A.4    Nawrot, B.5    Sochacka, E.6
  • 74
  • 75
    • 0024362769 scopus 로고
    • Ribonucleoside analysis by reversed-phase high-performance liquid chromatography
    • Gehrke C.W., Kuo K.C. Ribonucleoside analysis by reversed-phase high-performance liquid chromatography. J. Chromatog. 471:1989;3-36.
    • (1989) J. Chromatog. , vol.471 , pp. 3-36
    • Gehrke, C.W.1    Kuo, K.C.2
  • 76
    • 0029100233 scopus 로고
    • Predicting thermodynamic properties of RNA
    • Serra M.J., Turner D.H. Predicting thermodynamic properties of RNA. Methods Enzymol. 249:1995;242-261.
    • (1995) Methods Enzymol. , vol.249 , pp. 242-261
    • Serra, M.J.1    Turner, D.H.2
  • 77
    • 33646376290 scopus 로고
    • Spin diffusion measurements: Spin echoes in the presence of a time-dependent field gradient
    • Stejskal E.O., Tanner J.E. Spin diffusion measurements: spin echoes in the presence of a time-dependent field gradient. J. Chem. Phys. 42:1965;288-292.
    • (1965) J. Chem. Phys. , vol.42 , pp. 288-292
    • Stejskal, E.O.1    Tanner, J.E.2
  • 78
    • 36849101148 scopus 로고
    • Use of the stimulated echo in NMR diffusion studies
    • Tanner J.E. Use of the stimulated echo in NMR diffusion studies. J. Chem. Phys. 52:1970;2523-2626.
    • (1970) J. Chem. Phys. , vol.52 , pp. 2523-2626
    • Tanner, J.E.1
  • 79
    • 0031241810 scopus 로고    scopus 로고
    • Measurement of diffusion constants for nucleic acids by NMR
    • Lapham J., Rife J.P., Moore P.B., Crothers D.M. Measurement of diffusion constants for nucleic acids by NMR. J. Biomol. NMR. 10:1997;255-262.
    • (1997) J. Biomol. NMR , vol.10 , pp. 255-262
    • Lapham, J.1    Rife, J.P.2    Moore, P.B.3    Crothers, D.M.4
  • 80
    • 0000521134 scopus 로고
    • Spin-echo water suppression for the generation of pure-phase two-dimensional NMR spectra
    • Sklenar V., Bax A. Spin-echo water suppression for the generation of pure-phase two-dimensional NMR spectra. J. Magn. Reson. 74:1987;469-479.
    • (1987) J. Magn. Reson. , vol.74 , pp. 469-479
    • Sklenar, V.1    Bax, A.2
  • 81
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 82
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R.R., Wuthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1980;1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 83
    • 84915716471 scopus 로고
    • Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy
    • Macura S., Ernst R.R. Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41:1980;95-117.
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 84
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini U., Sorensen O.W., Ernst R.R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104:1982;6800-6801.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sorensen, O.W.2    Ernst, R.R.3
  • 85
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., Davis D.G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 86
    • 0024282849 scopus 로고
    • Clean TOCSY for proton spin system identification in macromolecules
    • Griesinger C., Otting G., Wuthrich K., Ernst R.R. Clean TOCSY for proton spin system identification in macromolecules. J. Am. Chem. Soc. 110:1988;7870-7872.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7870-7872
    • Griesinger, C.1    Otting, G.2    Wuthrich, K.3    Ernst, R.R.4
  • 87
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • Palmer A.G. III, Cavanagh J., Wright P.E., Rance J. Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J. Magn. Reson. 93:1991;151-170.
    • (1991) J. Magn. Reson. , vol.93 , pp. 151-170
    • Palmer III, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, J.4
  • 88
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer P., Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 89
    • 0023046345 scopus 로고
    • Assignment of the 31P and 1H resonances in oligonucleotides by two-dimensional NMR spectroscopy
    • Sklenar V., Miyashiro H., Zon G., Miles H.T., Bas A. Assignment of the 31P and 1H resonances in oligonucleotides by two-dimensional NMR spectroscopy. FEBS Letters. 208:1986;94-98.
    • (1986) FEBS Letters , vol.208 , pp. 94-98
    • Sklenar, V.1    Miyashiro, H.2    Zon, G.3    Miles, H.T.4    Bas, A.5
  • 90
    • 0000106980 scopus 로고
    • Two-dimensional hetero-TOCSY-NOESY. Correlation of phosphorus-31 resonances with anomeric and aromatic proton resonances in RNA
    • Kellogg G.W., Szewczak A.A., Moore P.B. Two-dimensional hetero-TOCSY-NOESY. Correlation of phosphorus-31 resonances with anomeric and aromatic proton resonances in RNA. J. Am. Chem. Soc. 114:1992;2727-2728.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2727-2728
    • Kellogg, G.W.1    Szewczak, A.A.2    Moore, P.B.3
  • 91
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • Wuthrich K., Billeter M., Braun W. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169:1983;949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wuthrich, K.1    Billeter, M.2    Braun, W.3
  • 92
    • 0028909308 scopus 로고
    • Novel techniques in nuclear magnetic resonance for nucleic acids
    • Aboul-ela F., Varani G. Novel techniques in nuclear magnetic resonance for nucleic acids. Curr. Opin. Biotechnol. 6:1995;89-95.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 89-95
    • Aboul-Ela, F.1    Varani, G.2
  • 94
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner S.J., Kollman P.A., Nguyen D.T., Case D.A. An all atom force field for simulations of proteins and nucleic acids. J. Comput. Chem. 7:1986;230-253.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-253
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.