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Volumn 365, Issue 2, 2007, Pages 411-424

Insights into Molecular Plasticity of Choline Binding Proteins (Pneumococcal Surface Proteins) by SAXS

Author keywords

analytical ultracentrifugation; choline binding proteins; protein flexibility; small angle X ray scattering; three dimensional solution structure

Indexed keywords

AMIDASE; BACTERIAL PROTEIN; BINDING PROTEIN; CHOLINE DERIVATIVE; MEMBRANE PROTEIN; MONOMER; PHOSPHORYLCHOLINE;

EID: 33751529207     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.09.091     Document Type: Article
Times cited : (20)

References (58)
  • 1
    • 33644840065 scopus 로고    scopus 로고
    • A pathogenic categorization of clinical syndromes caused by Streptococcus pneumoniae
    • Tuomanen E.I., Mitchell T.J., Morrison D.A., and Spratt B.G. (Eds), American Society for Microbiology Press, Washington, DC
    • Musher D.M. A pathogenic categorization of clinical syndromes caused by Streptococcus pneumoniae. In: Tuomanen E.I., Mitchell T.J., Morrison D.A., and Spratt B.G. (Eds). Pneumococcus (2004), American Society for Microbiology Press, Washington, DC 211-220
    • (2004) Pneumococcus , pp. 211-220
    • Musher, D.M.1
  • 2
    • 33644841084 scopus 로고
    • Choline, pantothenic acid and nicotinic acid as essential growth factors for pneumococcus
    • Rane L., and Subbarow Y. Choline, pantothenic acid and nicotinic acid as essential growth factors for pneumococcus. J. Biol. Chem. 134 (1940) 455-456
    • (1940) J. Biol. Chem. , vol.134 , pp. 455-456
    • Rane, L.1    Subbarow, Y.2
  • 3
    • 0014200202 scopus 로고
    • Choline in the cell wall of a bacterium: a novel type of polymer-linked choline in pneumococcus
    • Tomasz A. Choline in the cell wall of a bacterium: a novel type of polymer-linked choline in pneumococcus. Science 157 (1967) 694-697
    • (1967) Science , vol.157 , pp. 694-697
    • Tomasz, A.1
  • 4
    • 7944231131 scopus 로고    scopus 로고
    • Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage
    • López R., and García E. Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage. FEMS Microbiol. Rev. 28 (2004) 553-580
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 553-580
    • López, R.1    García, E.2
  • 5
    • 0025034304 scopus 로고
    • Pneumococcal surface protein A (PspA) is serologically highly variable and is expressed by all clinically important capsular serotypes of Streptococcus pneumoniae
    • Crain M.J., Waltman II W.D., Turner J.S., Yother J., Talkington D.F., McDaniel L.S., et al. Pneumococcal surface protein A (PspA) is serologically highly variable and is expressed by all clinically important capsular serotypes of Streptococcus pneumoniae. Infect. Immun. 58 (1990) 3293-3299
    • (1990) Infect. Immun. , vol.58 , pp. 3293-3299
    • Crain, M.J.1    Waltman II, W.D.2    Turner, J.S.3    Yother, J.4    Talkington, D.F.5    McDaniel, L.S.6
  • 6
    • 0030983804 scopus 로고    scopus 로고
    • Contribution of novel choline-binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae
    • Rosenow C., Ryan P., Weiser J.N., Johnson S., Fontan P., Ortqvist A., and Masure H.R. Contribution of novel choline-binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae. Mol. Microbiol. 25 (1997) 819-829
    • (1997) Mol. Microbiol. , vol.25 , pp. 819-829
    • Rosenow, C.1    Ryan, P.2    Weiser, J.N.3    Johnson, S.4    Fontan, P.5    Ortqvist, A.6    Masure, H.R.7
  • 7
    • 0030968621 scopus 로고    scopus 로고
    • SpsA, a novel pneumococcal surface protein with specific binding to secretory immunoglobulin A and secretory component
    • Hammerschmidt S., Talay S.R., Brandtzaeg P., and Chhatwal G.S. SpsA, a novel pneumococcal surface protein with specific binding to secretory immunoglobulin A and secretory component. Mol. Microbiol. 25 (1997) 1113-1124
    • (1997) Mol. Microbiol. , vol.25 , pp. 1113-1124
    • Hammerschmidt, S.1    Talay, S.R.2    Brandtzaeg, P.3    Chhatwal, G.S.4
  • 8
    • 0032721182 scopus 로고    scopus 로고
    • The pspC gene of Streptococcus pneumoniae encodes a polymorphic protein, PspC, with elicits cross-reactive antibodies to PspA and provides immunity to pneumococcal bacteraemia
    • Brooks-Walter A., Briles D.E., and Hollingshead S.K. The pspC gene of Streptococcus pneumoniae encodes a polymorphic protein, PspC, with elicits cross-reactive antibodies to PspA and provides immunity to pneumococcal bacteraemia. Infect. Immun. 67 (1999) 6533-6542
    • (1999) Infect. Immun. , vol.67 , pp. 6533-6542
    • Brooks-Walter, A.1    Briles, D.E.2    Hollingshead, S.K.3
  • 9
    • 0032797913 scopus 로고    scopus 로고
    • Pneumococcal surface protein A inhibits complement activation by Streptococcus pneumoniae
    • Tu A.H., Fulgham R.L., McCroy M.A., Briles D.E., and Szalai A.J. Pneumococcal surface protein A inhibits complement activation by Streptococcus pneumoniae. Infect. Immun. 67 (1999) 4720-4724
    • (1999) Infect. Immun. , vol.67 , pp. 4720-4724
    • Tu, A.H.1    Fulgham, R.L.2    McCroy, M.A.3    Briles, D.E.4    Szalai, A.J.5
  • 10
    • 0033796622 scopus 로고    scopus 로고
    • Role of novel choline binding proteins in virulence of Streptococcus pneumoniae
    • Gosink K.K., Mann E.R., Guglielmo C., Tuomanen E., and Masure R. Role of novel choline binding proteins in virulence of Streptococcus pneumoniae. Infect. Immun. 68 (2000) 5690-5695
    • (2000) Infect. Immun. , vol.68 , pp. 5690-5695
    • Gosink, K.K.1    Mann, E.R.2    Guglielmo, C.3    Tuomanen, E.4    Masure, R.5
  • 13
    • 0030994515 scopus 로고    scopus 로고
    • Bacteriophages of Streptococcus pneumoniae: a molecular approach
    • García P., Martín A.C., and López R. Bacteriophages of Streptococcus pneumoniae: a molecular approach. Microb. Drug Resist. 3 (1997) 165-176
    • (1997) Microb. Drug Resist. , vol.3 , pp. 165-176
    • García, P.1    Martín, A.C.2    López, R.3
  • 15
    • 0034282873 scopus 로고    scopus 로고
    • Do sequence repeats play an equivalent role in the choline-binding module of pneumococcal LytA amidase?
    • Varea J., Sáiz J.L., López-Zumel C., Monterroso B., Medrano F.J., Arrondo J.L.R., et al. Do sequence repeats play an equivalent role in the choline-binding module of pneumococcal LytA amidase?. J. Biol. Chem. 275 (2000) 20496-20501
    • (2000) J. Biol. Chem. , vol.275 , pp. 20496-20501
    • Varea, J.1    Sáiz, J.L.2    López-Zumel, C.3    Monterroso, B.4    Medrano, F.J.5    Arrondo, J.L.R.6
  • 16
    • 0036084635 scopus 로고    scopus 로고
    • Characterization of Ejl, the cell-wall amidase coded by the pneumococcal bacteriophage Ej-1
    • Sáiz J.L., López-Zumel C., Monterroso B., Varea J., Arrondo J.L.R., Iloro I., et al. Characterization of Ejl, the cell-wall amidase coded by the pneumococcal bacteriophage Ej-1. Protein Sci. 11 (2002) 1788-1799
    • (2002) Protein Sci. , vol.11 , pp. 1788-1799
    • Sáiz, J.L.1    López-Zumel, C.2    Monterroso, B.3    Varea, J.4    Arrondo, J.L.R.5    Iloro, I.6
  • 18
    • 0023551487 scopus 로고
    • 3′-end modification of the Streptococcus pneumoniae lytA gene: role of the carboxy terminus of the pneumococcal autolysin in the process of enzymatic activation (conversion)
    • Sánchez-Puelles J.M., García J.L., López R., and García E. 3′-end modification of the Streptococcus pneumoniae lytA gene: role of the carboxy terminus of the pneumococcal autolysin in the process of enzymatic activation (conversion). Gene 61 (1987) 13-19
    • (1987) Gene , vol.61 , pp. 13-19
    • Sánchez-Puelles, J.M.1    García, J.L.2    López, R.3    García, E.4
  • 19
    • 0026546261 scopus 로고
    • Studies on the structure and function of the N-terminal domain of the pneumococcal murein hydrolases
    • Sanz J.M., Díaz E., and García J.L. Studies on the structure and function of the N-terminal domain of the pneumococcal murein hydrolases. Mol. Microbiol. 6 (1992) 921-931
    • (1992) Mol. Microbiol. , vol.6 , pp. 921-931
    • Sanz, J.M.1    Díaz, E.2    García, J.L.3
  • 20
    • 22444442099 scopus 로고    scopus 로고
    • Insights into pneumococcal pathogenesis from the crystal structure of the modular teichoic acid phosphorylcholine esterase Pce
    • Hermoso J.A., Lagartera L., González A., Stelter M., García P., Martínez-Ripoll M., et al. Insights into pneumococcal pathogenesis from the crystal structure of the modular teichoic acid phosphorylcholine esterase Pce. Nature Struct. Mol. Biol. 12 (2005) 533-538
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 533-538
    • Hermoso, J.A.1    Lagartera, L.2    González, A.3    Stelter, M.4    García, P.5    Martínez-Ripoll, M.6
  • 22
    • 0141594766 scopus 로고    scopus 로고
    • Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1
    • Hermoso J.A., Monterroso B., Albert A., Galán B., Ahrazem O., García P., et al. Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. Structure 11 (2003) 1239-1249
    • (2003) Structure , vol.11 , pp. 1239-1249
    • Hermoso, J.A.1    Monterroso, B.2    Albert, A.3    Galán, B.4    Ahrazem, O.5    García, P.6
  • 23
    • 0035191795 scopus 로고    scopus 로고
    • Molecular characterization of the pneumococcal teichoic acid phosphorylcholine esterase
    • de las Rivas B., García J.L., López R., and García P. Molecular characterization of the pneumococcal teichoic acid phosphorylcholine esterase. Microb. Drug Res. 7 (2001) 213-222
    • (2001) Microb. Drug Res. , vol.7 , pp. 213-222
    • de las Rivas, B.1    García, J.L.2    López, R.3    García, P.4
  • 24
    • 0035061124 scopus 로고    scopus 로고
    • Identification of the teichoic acid phosphorylcholine esterase in Streptococcus pneumoniae
    • Vollmer W., and Tomasz A. Identification of the teichoic acid phosphorylcholine esterase in Streptococcus pneumoniae. Mol. Microbiol. 39 (2001) 1610-1622
    • (2001) Mol. Microbiol. , vol.39 , pp. 1610-1622
    • Vollmer, W.1    Tomasz, A.2
  • 25
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution
    • Koch M.H., Vachette P., and Svergun D.I. Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Quart. Rev. Biophys. 36 (2003) 147-227
    • (2003) Quart. Rev. Biophys. , vol.36 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 27
    • 0033525835 scopus 로고    scopus 로고
    • Conformational changes in the chaperonin GroEL: new insights into the allosteric mechanism
    • de Groot B.L., Vriend G., and Berendsen H.J. Conformational changes in the chaperonin GroEL: new insights into the allosteric mechanism. J. Mol. Biol. 286 (1999) 1241-1249
    • (1999) J. Mol. Biol. , vol.286 , pp. 1241-1249
    • de Groot, B.L.1    Vriend, G.2    Berendsen, H.J.3
  • 28
    • 0037008738 scopus 로고    scopus 로고
    • Mechanism of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. Structures of complexes with the substrate
    • Jedrzejas M.J., Mello L.V., de Groot B.L., and Li S. Mechanism of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. Structures of complexes with the substrate. J. Biol. Chem. 277 (2002) 28287-28297
    • (2002) J. Biol. Chem. , vol.277 , pp. 28287-28297
    • Jedrzejas, M.J.1    Mello, L.V.2    de Groot, B.L.3    Li, S.4
  • 29
    • 0037183993 scopus 로고    scopus 로고
    • Structure and flexibility of Streptococcus agalactiae hyaluronate lyase complex with its substrate. Insights into the mechanism of processive degradation of hyaluronan
    • Mello L.V., De Groot B.L., Li S., and Jedrzejas M.J. Structure and flexibility of Streptococcus agalactiae hyaluronate lyase complex with its substrate. Insights into the mechanism of processive degradation of hyaluronan. J. Biol. Chem. 277 (2002) 36678-36688
    • (2002) J. Biol. Chem. , vol.277 , pp. 36678-36688
    • Mello, L.V.1    De Groot, B.L.2    Li, S.3    Jedrzejas, M.J.4
  • 30
    • 1242338103 scopus 로고    scopus 로고
    • Conformational sampling for the impatient
    • Tai K. Conformational sampling for the impatient. Biophys. Chem. 107 (2004) 213-220
    • (2004) Biophys. Chem. , vol.107 , pp. 213-220
    • Tai, K.1
  • 31
    • 0242418195 scopus 로고    scopus 로고
    • Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling
    • Rigden D.J., Lamani E., Mello L.V., Littlejohn J.E., and Jedrzejas M.J. Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling. J. Mol. Biol. 328 (2003) 909-920
    • (2003) J. Mol. Biol. , vol.328 , pp. 909-920
    • Rigden, D.J.1    Lamani, E.2    Mello, L.V.3    Littlejohn, J.E.4    Jedrzejas, M.J.5
  • 33
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 34
    • 0034705330 scopus 로고    scopus 로고
    • Reconstruction of protein form with X-ray solution scattering and a genetic algorithm
    • Chacón P., Díaz J.F., Morán F., and Andreu J.M. Reconstruction of protein form with X-ray solution scattering and a genetic algorithm. J. Mol. Biol. 299 (2000) 1289-1302
    • (2000) J. Mol. Biol. , vol.299 , pp. 1289-1302
    • Chacón, P.1    Díaz, J.F.2    Morán, F.3    Andreu, J.M.4
  • 35
    • 0034849689 scopus 로고    scopus 로고
    • MASSHA - a graphics system for rigid-body modelling of macromolecular complexes against solution scattering data
    • Konarev P.V., Petoukhov M.V., and Svergun D.I. MASSHA - a graphics system for rigid-body modelling of macromolecular complexes against solution scattering data. J. Appl. Crystallog. 34 (2001) 527-532
    • (2001) J. Appl. Crystallog. , vol.34 , pp. 527-532
    • Konarev, P.V.1    Petoukhov, M.V.2    Svergun, D.I.3
  • 37
    • 27944474120 scopus 로고    scopus 로고
    • Choline binding proteins
    • Tuomanen E.I., Mitchell t.J., Morrison D.A., and Spratt B.G. (Eds), American Society for Microbiology Press, Washington, DC
    • Swiatlo E., McDaniels L.S., and Briles D.E. Choline binding proteins. In: Tuomanen E.I., Mitchell t.J., Morrison D.A., and Spratt B.G. (Eds). The Pneumococcus (2004), American Society for Microbiology Press, Washington, DC 49-60
    • (2004) The Pneumococcus , pp. 49-60
    • Swiatlo, E.1    McDaniels, L.S.2    Briles, D.E.3
  • 38
    • 0035943705 scopus 로고    scopus 로고
    • A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 Å resolution
    • Rau A., Hogg T., Marquardt R., and Hilgenfeld R. A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 Å resolution. J. Biol. Chem. 276 (2001) 31994-31999
    • (2001) J. Biol. Chem. , vol.276 , pp. 31994-31999
    • Rau, A.1    Hogg, T.2    Marquardt, R.3    Hilgenfeld, R.4
  • 39
    • 0026546261 scopus 로고
    • Studies on the structure and function of the N-terminal domain of the pneumococcal murein hydrolases
    • Sanz J.M., Díaz E., and García J.L. Studies on the structure and function of the N-terminal domain of the pneumococcal murein hydrolases. Mol. Microbiol. 6 (1992) 921-931
    • (1992) Mol. Microbiol. , vol.6 , pp. 921-931
    • Sanz, J.M.1    Díaz, E.2    García, J.L.3
  • 40
    • 0036349994 scopus 로고    scopus 로고
    • Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer
    • Fernández-Tornero C., García E., López R., Giménez-Gallego G., and Romero A. Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer. J. Mol. Biol. 321 (2002) 163-173
    • (2002) J. Mol. Biol. , vol.321 , pp. 163-173
    • Fernández-Tornero, C.1    García, E.2    López, R.3    Giménez-Gallego, G.4    Romero, A.5
  • 42
    • 0032995471 scopus 로고    scopus 로고
    • Molecular and cellular biology of pneumococcal infection
    • Tuomanen E. Molecular and cellular biology of pneumococcal infection. Curr. Opin. Microbiol. 2 (1999) 35-39
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 35-39
    • Tuomanen, E.1
  • 43
    • 33751551884 scopus 로고    scopus 로고
    • de las Rivas, B. (2002). Aislamiento y caracterización de nuevas proteínas de union a colina de Streptococcus pneumoniae. PhD Thesis, Universidad Complutense de Madrid.
  • 44
    • 0024295204 scopus 로고
    • Structural requirements of choline derivatives for "conversion" of pneumococcal amidase
    • Sanz J.M., López R., and García J.L. Structural requirements of choline derivatives for "conversion" of pneumococcal amidase. FEBS Letters 232 (1988) 308-312
    • (1988) FEBS Letters , vol.232 , pp. 308-312
    • Sanz, J.M.1    López, R.2    García, J.L.3
  • 45
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low-molecular weight solutes
    • Philo J. An improved function for fitting sedimentation velocity data for low-molecular weight solutes. Biophys. J. 72 (1997) 435-444
    • (1997) Biophys. J. , vol.72 , pp. 435-444
    • Philo, J.1
  • 46
    • 0013575443 scopus 로고
    • Sedimentation
    • Prentice May, Englewood Cliffs, NJ
    • van Holde K.E. Sedimentation. Physical Biochemistry (1985), Prentice May, Englewood Cliffs, NJ 110-136
    • (1985) Physical Biochemistry , pp. 110-136
    • van Holde, K.E.1
  • 47
    • 0027419731 scopus 로고
    • Human factor VIIa and its complex with soluble tissue factor: evaluation of asymmetry and conformational dynamics by ultracentrifugation and fluorescence anisotropy decay methods
    • Waxman E., Laws W.R., Laue T.M., Nemerson Y., and Ross J.B. Human factor VIIa and its complex with soluble tissue factor: evaluation of asymmetry and conformational dynamics by ultracentrifugation and fluorescence anisotropy decay methods. Biochemistry 32 (1993) 3005-3012
    • (1993) Biochemistry , vol.32 , pp. 3005-3012
    • Waxman, E.1    Laws, W.R.2    Laue, T.M.3    Nemerson, Y.4    Ross, J.B.5
  • 48
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding S.E., Rowe A.J., and Horton J.C. (Eds), Royal Society of Chemistry, Cambridge
    • Laue T.M., Shah B.D., Ridgeway T.M., and Pelletier S.L. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding S.E., Rowe A.J., and Horton J.C. (Eds). Analytical Ultracentrifugation in Biochemistry and Polymer Science (1992), Royal Society of Chemistry, Cambridge 90-125
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 50
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García de la Torre J., Huertas M.L., and Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78 (2000) 719-730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • García de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 51
    • 0031807272 scopus 로고    scopus 로고
    • Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm
    • Chacón P., Morán F., Díaz J.F., Pantos E., and Andreu J.M. Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm. Biophys. J. 74 (1998) 2760-2775
    • (1998) Biophys. J. , vol.74 , pp. 2760-2775
    • Chacón, P.1    Morán, F.2    Díaz, J.F.3    Pantos, E.4    Andreu, J.M.5
  • 52
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in Indirect-Transform Methods usong perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in Indirect-Transform Methods usong perceptual criteria. J. Appl. Crystallog. 25 (1992) 495-503
    • (1992) J. Appl. Crystallog. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 53
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallog. 36 (2003) 860-864
    • (2003) J. Appl. Crystallog. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 54
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallog. 28 (1995) 768-773
    • (1995) J. Appl. Crystallog. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 55
    • 0035209087 scopus 로고    scopus 로고
    • Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering
    • Wriggers W., and Chacón P. Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering. J. Appl. Crystallog. 34 (2001) 773-776
    • (2001) J. Appl. Crystallog. , vol.34 , pp. 773-776
    • Wriggers, W.1    Chacón, P.2
  • 56
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., and van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7 (2001) 306-317
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 57
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme
    • Hayward S., and Berendsen H.J. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins: Struct. Funct. Genet. 30 (1998) 144-154
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 58
    • 0036888353 scopus 로고    scopus 로고
    • Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50
    • Hayward S., and Lee R.A. Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50. J. Mol. Graph. Model. 21 (2002) 181-183
    • (2002) J. Mol. Graph. Model. , vol.21 , pp. 181-183
    • Hayward, S.1    Lee, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.