메뉴 건너뛰기




Volumn 378, Issue 1, 2008, Pages 165-177

Solution Structure and Dynamics of Peptidyl-tRNA Hydrolase from Mycobacterium tuberculosis H37Rv

Author keywords

backbone dynamics; Mycobacterium tuberculosis H37Rv; NMR; peptidyl tRNA hydrolase; protein structure

Indexed keywords

BACTERIAL ENZYME; HELIX LOOP HELIX PROTEIN; HYDROLASE; NITROGEN 15; PEPTIDYL TRNA HYDROLASE; UNCLASSIFIED DRUG;

EID: 41149093856     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.027     Document Type: Article
Times cited : (38)

References (59)
  • 1
    • 0022147039 scopus 로고
    • Constraints on the accuracy of RNA movement
    • Kurland C., and Ehrenberg M. Constraints on the accuracy of RNA movement. Quart. Rev. Biophys. 18 (1985) 423-450
    • (1985) Quart. Rev. Biophys. , vol.18 , pp. 423-450
    • Kurland, C.1    Ehrenberg, M.2
  • 2
    • 0038351296 scopus 로고    scopus 로고
    • Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome
    • Heurgue-Hamard V., Karimi R., Mora L., MacDougall J., Leboeuf C., Grentzmann G., et al. Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome. EMBO J. 17 (1998) 808-816
    • (1998) EMBO J. , vol.17 , pp. 808-816
    • Heurgue-Hamard, V.1    Karimi, R.2    Mora, L.3    MacDougall, J.4    Leboeuf, C.5    Grentzmann, G.6
  • 3
    • 0035996759 scopus 로고    scopus 로고
    • Expression, purification and characterization of peptidyl tRNA hydrolase from Staphylococcus aureus
    • Bonin P.D., Choi G.H., Trepod C.M., Mott J.E., Lyle S.B., Cialdella J.I., et al. Expression, purification and characterization of peptidyl tRNA hydrolase from Staphylococcus aureus. Protein Expr. Purif. 24 (2002) 123-130
    • (2002) Protein Expr. Purif. , vol.24 , pp. 123-130
    • Bonin, P.D.1    Choi, G.H.2    Trepod, C.M.3    Mott, J.E.4    Lyle, S.B.5    Cialdella, J.I.6
  • 4
    • 0032516787 scopus 로고    scopus 로고
    • Initiation factors IF1 and IF2 synergistically remove peptidyl-tRNAs with short polypeptides from the P-site of translating Escherichia coli ribosomes
    • Karimi R., Pavlov M.Y., Heurgue-Hamard V., Buckingham R.H., and Ehrenberg M. Initiation factors IF1 and IF2 synergistically remove peptidyl-tRNAs with short polypeptides from the P-site of translating Escherichia coli ribosomes. J. Mol. Biol. 281 (1998) 241-252
    • (1998) J. Mol. Biol. , vol.281 , pp. 241-252
    • Karimi, R.1    Pavlov, M.Y.2    Heurgue-Hamard, V.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 5
    • 0018127496 scopus 로고
    • The accumulation as peptidyl-transfer RNA of isoaccepting transfer RNA families in Escherichia coli with temperature-sensitive peptidyl-transfer RNA hydrolase
    • Menninger J.R. The accumulation as peptidyl-transfer RNA of isoaccepting transfer RNA families in Escherichia coli with temperature-sensitive peptidyl-transfer RNA hydrolase. J. Biol. Chem. 253 (1978) 6808-6813
    • (1978) J. Biol. Chem. , vol.253 , pp. 6808-6813
    • Menninger, J.R.1
  • 6
    • 0037492900 scopus 로고    scopus 로고
    • The rate of peptidyl-tRNA dissociation from the ribosome during minigene expression depends on the nature of the last decoding interaction
    • Cruz-Vera L.R., Ramon E.H., Zamorano B.P., and Guarneros G. The rate of peptidyl-tRNA dissociation from the ribosome during minigene expression depends on the nature of the last decoding interaction. J. Biol. Chem. 278 (2003) 26065-26070
    • (2003) J. Biol. Chem. , vol.278 , pp. 26065-26070
    • Cruz-Vera, L.R.1    Ramon, E.H.2    Zamorano, B.P.3    Guarneros, G.4
  • 7
    • 0038351297 scopus 로고    scopus 로고
    • Lambda bar minigene-mediated inhibition of protein synthesis involves accumulation of peptidyl-tRNA and starvation for tRNA
    • Hernandez-Sanchez J., Valadez J.G., Herrera J.V., Ontiveros C., and Guarneros G. Lambda bar minigene-mediated inhibition of protein synthesis involves accumulation of peptidyl-tRNA and starvation for tRNA. EMBO J. 17 (1998) 3758-3765
    • (1998) EMBO J. , vol.17 , pp. 3758-3765
    • Hernandez-Sanchez, J.1    Valadez, J.G.2    Herrera, J.V.3    Ontiveros, C.4    Guarneros, G.5
  • 8
  • 9
    • 0040559883 scopus 로고    scopus 로고
    • Quality control mechanisms during translation
    • Ibba M., and Soll D. Quality control mechanisms during translation. Science 286 (1999) 1893-1897
    • (1999) Science , vol.286 , pp. 1893-1897
    • Ibba, M.1    Soll, D.2
  • 10
    • 0018340811 scopus 로고
    • Accumulation of peptidyl tRNA is lethal to Escherichia coli
    • Menninger J.R. Accumulation of peptidyl tRNA is lethal to Escherichia coli. J. Bacteriol. 137 (1979) 694-696
    • (1979) J. Bacteriol. , vol.137 , pp. 694-696
    • Menninger, J.R.1
  • 11
    • 0034006502 scopus 로고    scopus 로고
    • Molecular basis for the temperature sensitivity of Escherichia coli pth(Ts)
    • Cruz-Vera L.R., Toledo I., Hernandez-Sanchez J., and Guarneros G. Molecular basis for the temperature sensitivity of Escherichia coli pth(Ts). J. Bacteriol. 182 (2000) 1523-1528
    • (2000) J. Bacteriol. , vol.182 , pp. 1523-1528
    • Cruz-Vera, L.R.1    Toledo, I.2    Hernandez-Sanchez, J.3    Guarneros, G.4
  • 12
    • 0017115214 scopus 로고
    • Peptidyl transfer RNA dissociates during protein synthesis from ribosomes of Escherichia coli
    • Menninger J.R. Peptidyl transfer RNA dissociates during protein synthesis from ribosomes of Escherichia coli. J. Biol. Chem. 251 (1976) 3392-3398
    • (1976) J. Biol. Chem. , vol.251 , pp. 3392-3398
    • Menninger, J.R.1
  • 13
    • 0029976654 scopus 로고    scopus 로고
    • The growth defect in Escherichia coli deficient in peptidyl-tRNA hydrolase is due to starvation for Lys-tRNA(Lys)
    • Heurgue-Hamard V., Mora L., Guarneros G., and Buckingham R.H. The growth defect in Escherichia coli deficient in peptidyl-tRNA hydrolase is due to starvation for Lys-tRNA(Lys). EMBO J. 15 (1996) 2826-2833
    • (1996) EMBO J. , vol.15 , pp. 2826-2833
    • Heurgue-Hamard, V.1    Mora, L.2    Guarneros, G.3    Buckingham, R.H.4
  • 14
    • 0034555130 scopus 로고    scopus 로고
    • Sequestration of specific tRNA species cognate to the last sense codon of an over produced gratuitous protein
    • Menez J., Heurgue-Hamard V., and Buckingham R.H. Sequestration of specific tRNA species cognate to the last sense codon of an over produced gratuitous protein. Nucleic Acids Res. 28 (2000) 4725-4732
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4725-4732
    • Menez, J.1    Heurgue-Hamard, V.2    Buckingham, R.H.3
  • 16
    • 0030738859 scopus 로고    scopus 로고
    • Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl tRNA hydrolase
    • Schmitt E., Mechulam Y., Fromant M., Plateau P., and Blanquet S. Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl tRNA hydrolase. EMBO J. 16 (1997) 4760-4769
    • (1997) EMBO J. , vol.16 , pp. 4760-4769
    • Schmitt, E.1    Mechulam, Y.2    Fromant, M.3    Plateau, P.4    Blanquet, S.5
  • 17
    • 9744223828 scopus 로고    scopus 로고
    • Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
    • Goodall J.J., Chen G.J., and Page M.G. Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase. Biochemistry 43 (2004) 4583-4591
    • (2004) Biochemistry , vol.43 , pp. 4583-4591
    • Goodall, J.J.1    Chen, G.J.2    Page, M.G.3
  • 18
    • 9744285756 scopus 로고    scopus 로고
    • Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces
    • Ostheimer G.J., Hadjivassiliou H., Kloer D.P., Barkan A., and Matthews B.W. Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces. J. Mol. Biol. 345 (2005) 51-68
    • (2005) J. Mol. Biol. , vol.345 , pp. 51-68
    • Ostheimer, G.J.1    Hadjivassiliou, H.2    Kloer, D.P.3    Barkan, A.4    Matthews, B.W.5
  • 19
    • 1542289663 scopus 로고    scopus 로고
    • Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity
    • De Pereda J.M., Waas W.F., Jan Y., Ruoslahti E., Schimmel P., and Pascual J. Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity. J. Biol. Chem. 279 (2004) 8111-8115
    • (2004) J. Biol. Chem. , vol.279 , pp. 8111-8115
    • De Pereda, J.M.1    Waas, W.F.2    Jan, Y.3    Ruoslahti, E.4    Schimmel, P.5    Pascual, J.6
  • 20
    • 15544363359 scopus 로고    scopus 로고
    • Crystal structure at 1.8 Å resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase
    • Fromant M., Schmitt E., Mechulam Y., Lazennec C., Plateau P., and Blanquet S. Crystal structure at 1.8 Å resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase. Biochemistry 44 (2005) 4294-4301
    • (2005) Biochemistry , vol.44 , pp. 4294-4301
    • Fromant, M.1    Schmitt, E.2    Mechulam, Y.3    Lazennec, C.4    Plateau, P.5    Blanquet, S.6
  • 21
    • 27644512847 scopus 로고    scopus 로고
    • Solution structure of Archaeglobus fulgidis peptidyl-tRNA hydrolase (Pth2) provides evidence for an extensive conserved family of Pth2 enzymes in archea, bacteria, and eukaryotes
    • Powers R., Mirkovic N., Goldsmith-Fischman S., Acton T.B., Chiang Y., Huang Y.J., et al. Solution structure of Archaeglobus fulgidis peptidyl-tRNA hydrolase (Pth2) provides evidence for an extensive conserved family of Pth2 enzymes in archea, bacteria, and eukaryotes. Protein Sci. 14 (2005) 2849-2861
    • (2005) Protein Sci. , vol.14 , pp. 2849-2861
    • Powers, R.1    Mirkovic, N.2    Goldsmith-Fischman, S.3    Acton, T.B.4    Chiang, Y.5    Huang, Y.J.6
  • 22
    • 1542289663 scopus 로고    scopus 로고
    • Crystal structure of a human Peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity
    • De Pereda J.M., Waas W.F., Jan Y., Ruoslahti E., Schimmel P., and Pascual J. Crystal structure of a human Peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity. J. Biol. Chem. 279 (2004) 8111-8115
    • (2004) J. Biol. Chem. , vol.279 , pp. 8111-8115
    • De Pereda, J.M.1    Waas, W.F.2    Jan, Y.3    Ruoslahti, E.4    Schimmel, P.5    Pascual, J.6
  • 24
    • 0026500398 scopus 로고
    • Purification and initial characterization of peptidyl-tRNA hydrolase from rabbit reticulocytes
    • Gross M., Starn T.K., Rundquist C., Crow P., White J., Olin A., and Wagner T. Purification and initial characterization of peptidyl-tRNA hydrolase from rabbit reticulocytes. J. Biol. Chem. 267 (1992) 2073-2079
    • (1992) J. Biol. Chem. , vol.267 , pp. 2073-2079
    • Gross, M.1    Starn, T.K.2    Rundquist, C.3    Crow, P.4    White, J.5    Olin, A.6    Wagner, T.7
  • 25
    • 0026567885 scopus 로고
    • The site of hydrolysis by rabbit reticulocyte peptidyl tRNA hydrolase is the 3′-AMP terminus of susceptible tRNA substrate
    • Gross W., Crow P., and White J. The site of hydrolysis by rabbit reticulocyte peptidyl tRNA hydrolase is the 3′-AMP terminus of susceptible tRNA substrate. J. Biol. Chem. 267 (1992) 2080-2086
    • (1992) J. Biol. Chem. , vol.267 , pp. 2080-2086
    • Gross, W.1    Crow, P.2    White, J.3
  • 26
    • 0015929629 scopus 로고
    • Studies on the metabolic role of peptidyl tRNA hydrolase I. Properties of a mutant E. coli with temperature sensitive peptidyl tRNA hydrolase
    • Menninger J.R., Walker C., and Tan P.F. Studies on the metabolic role of peptidyl tRNA hydrolase I. Properties of a mutant E. coli with temperature sensitive peptidyl tRNA hydrolase. Mol. Gen. Genet. 121 (1973) 307-324
    • (1973) Mol. Gen. Genet. , vol.121 , pp. 307-324
    • Menninger, J.R.1    Walker, C.2    Tan, P.F.3
  • 27
    • 31044452898 scopus 로고    scopus 로고
    • Identification of a nitroimidazo-oxazine-specific protein involved in PA-824 resistance in Mycobacterium tuberculosis
    • Manjunatha U.H., Boshoff H., Dowd C.S., Zhang L., Albert T.J., Norton J.E., et al. Identification of a nitroimidazo-oxazine-specific protein involved in PA-824 resistance in Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 103 (2006) 431-436
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 431-436
    • Manjunatha, U.H.1    Boshoff, H.2    Dowd, C.S.3    Zhang, L.4    Albert, T.J.5    Norton, J.E.6
  • 30
    • 0141960052 scopus 로고    scopus 로고
    • Intrinsic macrolide resistance in Mycobacterium smegmatis is conferred by a novel erm gene, erm(38)
    • Nash K.A. Intrinsic macrolide resistance in Mycobacterium smegmatis is conferred by a novel erm gene, erm(38). Antimicrob. Agents Chemother. 47 (2003) 3053-3060
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3053-3060
    • Nash, K.A.1
  • 31
    • 0020322533 scopus 로고
    • Erythromycin, carbomycin and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl tRNA from ribosomes
    • Menninger J.R., and Otto D.P. Erythromycin, carbomycin and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl tRNA from ribosomes. Antimicrob. Agents Chemother. 21 (1982) 811-818
    • (1982) Antimicrob. Agents Chemother. , vol.21 , pp. 811-818
    • Menninger, J.R.1    Otto, D.P.2
  • 32
    • 34249057098 scopus 로고    scopus 로고
    • Characterization of Peptidyl-tRNA hydrolase encoded by open reading frame Rv1014c of Mycobacterium tuberculosis H37Rv
    • Bal N.C., Agarwal H., Meher A.K., and Arora A. Characterization of Peptidyl-tRNA hydrolase encoded by open reading frame Rv1014c of Mycobacterium tuberculosis H37Rv. Biol. Chem. 388 (2007) 467-479
    • (2007) Biol. Chem. , vol.388 , pp. 467-479
    • Bal, N.C.1    Agarwal, H.2    Meher, A.K.3    Arora, A.4
  • 33
    • 34547683824 scopus 로고    scopus 로고
    • Structural plasticity and enzyme action: crystal structures of Mycobacterium tuberculosis peptidyl-tRNA hydrolase
    • Selvaraj M., Roy S., Singh N.S., Sangeetha R., Varshney U., and Vijayan M. Structural plasticity and enzyme action: crystal structures of Mycobacterium tuberculosis peptidyl-tRNA hydrolase. J. Mol. Biol. 372 (2007) 186-193
    • (2007) J. Mol. Biol. , vol.372 , pp. 186-193
    • Selvaraj, M.1    Roy, S.2    Singh, N.S.3    Sangeetha, R.4    Varshney, U.5    Vijayan, M.6
  • 35
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari G., and Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104 (1982) 4546-4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 36
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Theory and range of validity
    • Lipari G., and Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Theory and range of validity. J. Am. Chem. Soc. 104 (1982) 4559-4570
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 38
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., and Palmer A.G. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246 (1995) 144-163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 40
    • 0028674384 scopus 로고
    • Investigation of protein motions via relaxation measurements
    • Peng J.W., and Wagner G. Investigation of protein motions via relaxation measurements. Methods Enzymol. 239 (1994) 563-596
    • (1994) Methods Enzymol. , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 41
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol.NMR 8 (1996) 477-486
    • (1996) J. Biomol.NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 42
    • 0038068865 scopus 로고    scopus 로고
    • FAST-Modelfree: A program for rapid automated analysis of solution NMR spin relaxation data
    • Roger C., and Loria J.P. FAST-Modelfree: A program for rapid automated analysis of solution NMR spin relaxation data. J. Biomol. NMR 26 (2003) 203-213
    • (2003) J. Biomol. NMR , vol.26 , pp. 203-213
    • Roger, C.1    Loria, J.P.2
  • 43
    • 0041524212 scopus 로고    scopus 로고
    • Letter to the Editor: Resonance assignment and secondary structure of an N-terminal fragment of human La protein
    • Alfano C., Babon J., Kelly G., Curry S., and Conte M.R. Letter to the Editor: Resonance assignment and secondary structure of an N-terminal fragment of human La protein. J. Biomol. NMR 27 (2003) 93-94
    • (2003) J. Biomol. NMR , vol.27 , pp. 93-94
    • Alfano, C.1    Babon, J.2    Kelly, G.3    Curry, S.4    Conte, M.R.5
  • 44
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common aminoacids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common aminoacids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5 (1995) 67-81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 45
    • 0033586788 scopus 로고    scopus 로고
    • Receptor site for the 5′-phosphate of elongator tRNAs governs substrate selection by peptidyl tRNA hydrolase
    • Fromant M., Plateau P., Schmitt E., Mechulam Y., and Blanquet S. Receptor site for the 5′-phosphate of elongator tRNAs governs substrate selection by peptidyl tRNA hydrolase. Biochemistry 38 (1999) 4982-4987
    • (1999) Biochemistry , vol.38 , pp. 4982-4987
    • Fromant, M.1    Plateau, P.2    Schmitt, E.3    Mechulam, Y.4    Blanquet, S.5
  • 46
    • 0026319199 scopus 로고
    • GRASP: Graphical representation and analysis of surface potential properties
    • Nicholls A., Sharp K.A., and Honig B. GRASP: Graphical representation and analysis of surface potential properties. Proteins. Struct. Funct. Genet. 11 (1991) 281-285
    • (1991) Proteins. Struct. Funct. Genet. , vol.11 , pp. 281-285
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 47
    • 1042275603 scopus 로고    scopus 로고
    • Exploring the range of protein flexibility, from a structural proteomics perspective
    • Gerstein M., and Echols N. Exploring the range of protein flexibility, from a structural proteomics perspective. Curr. Opin. Chem. Biol. 8 (2004) 14-19
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 14-19
    • Gerstein, M.1    Echols, N.2
  • 48
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier A., and Kay L.E. New tools provide new insights in NMR studies of protein dynamics. Science 312 (2006) 224-228
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 49
    • 2942579193 scopus 로고    scopus 로고
    • The use of nuclear relaxation to probe molecular interactions
    • Atkinson R.A., and Kieffer B. The use of nuclear relaxation to probe molecular interactions. Prog. Nucl. Magn. Reson. Spectrosc. 44 (2004) 141-187
    • (2004) Prog. Nucl. Magn. Reson. Spectrosc. , vol.44 , pp. 141-187
    • Atkinson, R.A.1    Kieffer, B.2
  • 52
    • 0343459675 scopus 로고
    • The program XEASY for computer supported NMR spectral analysis of biological macromolecules
    • Bartels C., Xia T., Billeter M., Guntert P., and Wuthrich K. The program XEASY for computer supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6 (1995) 1-10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Guntert, P.4    Wuthrich, K.5
  • 53
    • 41149138533 scopus 로고    scopus 로고
    • Keller, R., (2005). Optimizing the Process of Nuclear Magnetic Resonance Spectrum Analysis and Computer Aided Resonance Assignment. Diss. ETH no. 15947, Swiss Federal Institute of Technology, Zurich.
    • Keller, R., (2005). Optimizing the Process of Nuclear Magnetic Resonance Spectrum Analysis and Computer Aided Resonance Assignment. Diss. ETH no. 15947, Swiss Federal Institute of Technology, Zurich.
  • 54
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 271 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.271 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 56
    • 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
  • 57
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 58
    • 12044256620 scopus 로고
    • Intramolecular motions of a zinc finger DNA binding domain from Xfin characterized by proton detected natural abundance C-12 heteronuclear NMR-spectroscopy
    • Palmer A.G., Rance M., and Wright P.E. Intramolecular motions of a zinc finger DNA binding domain from Xfin characterized by proton detected natural abundance C-12 heteronuclear NMR-spectroscopy. J. Am. Chem. Soc. 113 (1991) 4371-4380
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4371-4380
    • Palmer, A.G.1    Rance, M.2    Wright, P.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.