메뉴 건너뛰기




Volumn 10, Issue 6, 2016, Pages 5751-5758

Theoretical Study of the Initial Stages of Self-Assembly of a Carboxysome's Facet

Author keywords

all atomistic; carboxysome; coarse grain model; nucleation growth; potential of mean force; protein self assembly

Indexed keywords

D REGION; GRAIN GROWTH; INTELLIGENT SYSTEMS; MONTE CARLO METHODS; NUCLEATION; PLASMA INTERACTIONS; PROTEINS; SHELLS (STRUCTURES);

EID: 84976643061     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/acsnano.5b07805     Document Type: Article
Times cited : (19)

References (50)
  • 1
    • 49649111573 scopus 로고    scopus 로고
    • Protein-Based Organelles in Bacteria: Carboxysomes and Related Microcompartments
    • Yeates, T. O.; Kerfeld, C. A.; Heinhorst, S.; Cannon, G. C.; Shively, J. M. Protein-Based Organelles in Bacteria: Carboxysomes and Related Microcompartments Nat. Rev. Microbiol. 2008, 6, 681-691 10.1038/nrmicro1913
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 681-691
    • Yeates, T.O.1    Kerfeld, C.A.2    Heinhorst, S.3    Cannon, G.C.4    Shively, J.M.5
  • 2
    • 0037318701 scopus 로고    scopus 로고
    • CO2 Concentrating Mechanisms in Cyanobacteria: Molecular Components, Their Diversity and Evolution
    • Badger, M. R.; Price, G. D. CO2 Concentrating Mechanisms in Cyanobacteria: Molecular Components, Their Diversity and Evolution J. Exp. Bot. 2003, 54, 609-622 10.1093/jxb/erg076
    • (2003) J. Exp. Bot. , vol.54 , pp. 609-622
    • Badger, M.R.1    Price, G.D.2
  • 3
    • 84856963458 scopus 로고    scopus 로고
    • Comparative Analysis of Carboxysome Shell Proteins
    • Kinney, J. N.; Axen, S. D.; Kerfeld, C. A. Comparative Analysis of Carboxysome Shell Proteins Photosynth. Res. 2011, 109, 21-32 10.1007/s11120-011-9624-6
    • (2011) Photosynth. Res. , vol.109 , pp. 21-32
    • Kinney, J.N.1    Axen, S.D.2    Kerfeld, C.A.3
  • 5
    • 73149089710 scopus 로고    scopus 로고
    • Two-Dimensional Crystals of Carboxysome Shell Proteins Recapitulate the Hexagonal Packing of Three-Dimensional Crystals
    • Dryden, K. A.; Crowley, C. S.; Tanaka, S.; Yeates, T. O.; Yeager, M. Two-Dimensional Crystals of Carboxysome Shell Proteins Recapitulate the Hexagonal Packing of Three-Dimensional Crystals Protein Sci. 2009, 18, 2629-2635 10.1002/pro.272
    • (2009) Protein Sci. , vol.18 , pp. 2629-2635
    • Dryden, K.A.1    Crowley, C.S.2    Tanaka, S.3    Yeates, T.O.4    Yeager, M.5
  • 6
    • 84960532549 scopus 로고    scopus 로고
    • Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy
    • Sutter, M.; Faulkner, M.; Aussignargues, C.; Paasch, B. C.; Barrett, S.; Kerfeld, C. A.; Liu, L. Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy Nano Lett. 2015, 10.1021/acs.nanolett.5b04259
    • (2015) Nano Lett.
    • Sutter, M.1    Faulkner, M.2    Aussignargues, C.3    Paasch, B.C.4    Barrett, S.5    Kerfeld, C.A.6    Liu, L.7
  • 7
    • 33845204189 scopus 로고    scopus 로고
    • Stability and Dynamics of Virus Capsids Described by Coarse-Grained Modeling
    • Arkhipov, A.; Freddolino, P. L.; Schulten, K. Stability and Dynamics of Virus Capsids Described by Coarse-Grained Modeling Structure 2006, 14, 1767-1777 10.1016/j.str.2006.10.003
    • (2006) Structure , vol.14 , pp. 1767-1777
    • Arkhipov, A.1    Freddolino, P.L.2    Schulten, K.3
  • 8
    • 33646123091 scopus 로고    scopus 로고
    • Coarse-Grained Modeling of the Actin Filament Derived from Atomistic-Scale Simulations
    • Chu, J. W.; Voth, G. A. Coarse-Grained Modeling of the Actin Filament Derived from Atomistic-Scale Simulations Biophys. J. 2006, 90, 1572-1582 10.1529/biophysj.105.073924
    • (2006) Biophys. J. , vol.90 , pp. 1572-1582
    • Chu, J.W.1    Voth, G.A.2
  • 9
    • 39149100599 scopus 로고    scopus 로고
    • Coarse-Grained Models of Protein Folding: Toy Models or Predictive Tools?
    • Clementi, C. Coarse-Grained Models of Protein Folding: Toy Models or Predictive Tools? Curr. Opin. Struct. Biol. 2008, 18, 10-15 10.1016/j.sbi.2007.10.005
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 10-15
    • Clementi, C.1
  • 10
    • 0037079578 scopus 로고    scopus 로고
    • Dynamics of Large Proteins Through Hierarchical Levels of Coarse-Grained Structures
    • Doruker, P.; Jernigan, R. L.; Bahar, I. Dynamics of Large Proteins Through Hierarchical Levels of Coarse-Grained Structures J. Comput. Chem. 2002, 23, 119-127 10.1002/jcc.1160
    • (2002) J. Comput. Chem. , vol.23 , pp. 119-127
    • Doruker, P.1    Jernigan, R.L.2    Bahar, I.3
  • 11
    • 0037398844 scopus 로고    scopus 로고
    • Minimalist Models for Protein Folding and Design
    • Head-Gordon, T.; Brown, S. Minimalist Models for Protein Folding and Design Curr. Opin. Struct. Biol. 2003, 13, 160-167 10.1016/S0959-440X(03)00030-7
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 160-167
    • Head-Gordon, T.1    Brown, S.2
  • 12
    • 63449129633 scopus 로고    scopus 로고
    • Insights from Coarse-Grained Go Models for Protein Folding and Dynamics
    • Hills, R. D.; Brooks, C. L. Insights from Coarse-Grained Go Models for Protein Folding and Dynamics Int. J. Mol. Sci. 2009, 10, 889-905 10.3390/ijms10030889
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 889-905
    • Hills, R.D.1    Brooks, C.L.2
  • 13
    • 34548809141 scopus 로고    scopus 로고
    • A Coarse-Grained Protein Force Field for Folding and Structure Prediction
    • Maupetit, J.; Tuffery, P.; Derreumaux, P. A Coarse-Grained Protein Force Field for Folding and Structure Prediction Proteins: Struct., Funct., Genet. 2007, 69, 394-408 10.1002/prot.21505
    • (2007) Proteins: Struct., Funct., Genet. , vol.69 , pp. 394-408
    • Maupetit, J.1    Tuffery, P.2    Derreumaux, P.3
  • 14
    • 28844494903 scopus 로고    scopus 로고
    • Coarse-Grained Model of Proteins Incorporating Atomistic Detail of the Active Site
    • Neri, M.; Anselmi, C.; Cascella, M.; Maritan, A.; Carloni, P. Coarse-Grained Model of Proteins Incorporating Atomistic Detail of the Active Site Phys. Rev. Lett. 2005, 95, 218102 10.1103/PhysRevLett.95.218102
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 218102
    • Neri, M.1    Anselmi, C.2    Cascella, M.3    Maritan, A.4    Carloni, P.5
  • 15
    • 33847712647 scopus 로고    scopus 로고
    • Deciphering the Kinetic Mechanism of Spontaneous Self-Assembly of Icosahedral Capsids
    • Nguyen, H. D.; Reddy, V. S.; Brooks, C. L. Deciphering the Kinetic Mechanism of Spontaneous Self-Assembly of Icosahedral Capsids Nano Lett. 2007, 7, 338-344 10.1021/nl062449h
    • (2007) Nano Lett. , vol.7 , pp. 338-344
    • Nguyen, H.D.1    Reddy, V.S.2    Brooks, C.L.3
  • 16
    • 2342473866 scopus 로고    scopus 로고
    • Coarse Grain Models and the Computer Simulation of Soft Materials
    • Nielsen, S. O.; Lopez, C. F.; Srinivas, G.; Klein, M. L. Coarse Grain Models and the Computer Simulation of Soft Materials J. Phys.: Condens. Matter 2004, 16, R481-R512 10.1088/0953-8984/16/15/R03
    • (2004) J. Phys.: Condens. Matter , vol.16 , pp. R481-R512
    • Nielsen, S.O.1    Lopez, C.F.2    Srinivas, G.3    Klein, M.L.4
  • 17
    • 46149109506 scopus 로고    scopus 로고
    • The Multiscale Coarse-Graining Method. I. A Rigorous Bridge between Atomistic and Coarse-Grained Models
    • Noid, W. G.; Chu, J. W.; Ayton, G. S.; Krishna, V.; Izvekov, S.; Voth, G. A.; Das, A.; Andersen, H. C. The Multiscale Coarse-Graining Method. I. A Rigorous Bridge Between Atomistic and Coarse-Grained Models J. Chem. Phys. 2008, 128, 244114 10.1063/1.2938860
    • (2008) J. Chem. Phys. , vol.128 , pp. 244114
    • Noid, W.G.1    Chu, J.W.2    Ayton, G.S.3    Krishna, V.4    Izvekov, S.5    Voth, G.A.6    Das, A.7    Andersen, H.C.8
  • 18
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the Aggregation Kinetics of Amyloid Peptides
    • Pellarin, R.; Caflisch, A. Interpreting the Aggregation Kinetics of Amyloid Peptides J. Mol. Biol. 2006, 360, 882-892 10.1016/j.jmb.2006.05.033
    • (2006) J. Mol. Biol. , vol.360 , pp. 882-892
    • Pellarin, R.1    Caflisch, A.2
  • 19
    • 17044393884 scopus 로고    scopus 로고
    • Coarse-Grained Models for Proteins
    • Tozzini, V. Coarse-Grained Models for Proteins Curr. Opin. Struct. Biol. 2005, 15, 144-150 10.1016/j.sbi.2005.02.005
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 144-150
    • Tozzini, V.1
  • 20
    • 34548804689 scopus 로고    scopus 로고
    • Computational Simulations of the Early Steps of Protein Aggregation
    • Wei, G. H.; Mousseau, N.; Derreumaux, P. Computational Simulations of the Early Steps of Protein Aggregation Prion 2007, 1, 3-8 10.4161/pri.1.1.3969
    • (2007) Prion , vol.1 , pp. 3-8
    • Wei, G.H.1    Mousseau, N.2    Derreumaux, P.3
  • 21
    • 33847193915 scopus 로고    scopus 로고
    • Assembly of Lipoprotein Particles Revealed by Coarse-Grained Molecular Dynamics Simulations
    • Shih, A. Y.; Freddolino, P. L.; Arkhipov, A.; Schulten, K. Assembly of Lipoprotein Particles Revealed by Coarse-Grained Molecular Dynamics Simulations J. Struct. Biol. 2007, 157, 579-592 10.1016/j.jsb.2006.08.006
    • (2007) J. Struct. Biol. , vol.157 , pp. 579-592
    • Shih, A.Y.1    Freddolino, P.L.2    Arkhipov, A.3    Schulten, K.4
  • 22
    • 33646007703 scopus 로고    scopus 로고
    • Coarse-Grained Strategy for Modeling Protein Stability in Concentrated Solutions. II: Phase Behavior
    • Shen, V. K.; Cheung, J. K.; Errington, J. R.; Truskett, T. M. Coarse-Grained Strategy for Modeling Protein Stability in Concentrated Solutions. II: Phase Behavior Biophys. J. 2006, 90, 1949-1960 10.1529/biophysj.105.076497
    • (2006) Biophys. J. , vol.90 , pp. 1949-1960
    • Shen, V.K.1    Cheung, J.K.2    Errington, J.R.3    Truskett, T.M.4
  • 23
    • 33748770940 scopus 로고    scopus 로고
    • Minimalist Protein Model as a Diagnostic Tool for Misfolding and Aggregation
    • Matysiak, S.; Clementi, C. Minimalist Protein Model as a Diagnostic Tool for Misfolding and Aggregation J. Mol. Biol. 2006, 363, 297-308 10.1016/j.jmb.2006.07.088
    • (2006) J. Mol. Biol. , vol.363 , pp. 297-308
    • Matysiak, S.1    Clementi, C.2
  • 24
    • 77955487466 scopus 로고    scopus 로고
    • Multiscale Coarse-Graining of the Protein Energy Landscape
    • Hills, R. D.; Lu, L. Y.; Voth, G. A. Multiscale Coarse-Graining of the Protein Energy Landscape PLoS Comput. Biol. 2010, 6, e1000827 10.1371/journal.pcbi.1000827
    • (2010) PLoS Comput. Biol. , vol.6 , pp. e1000827
    • Hills, R.D.1    Lu, L.Y.2    Voth, G.A.3
  • 25
    • 77957965654 scopus 로고    scopus 로고
    • Extending the PRIME Model for Protein Aggregation to All 20 Amino Acids
    • Cheon, M.; Chang, I.; Hall, C. K. Extending the PRIME Model for Protein Aggregation to All 20 Amino Acids Proteins: Struct., Funct., Genet. 2010, 78, 2950-2960 10.1002/prot.22817
    • (2010) Proteins: Struct., Funct., Genet. , vol.78 , pp. 2950-2960
    • Cheon, M.1    Chang, I.2    Hall, C.K.3
  • 26
    • 0035151879 scopus 로고    scopus 로고
    • Competition between Protein Folding and Aggregation: A Three-Dimensional Lattice-Model Simulation
    • Bratko, D.; Blanch, H. W. Competition Between Protein Folding and Aggregation: A Three-Dimensional Lattice-Model Simulation J. Chem. Phys. 2001, 114, 561-569 10.1063/1.1330212
    • (2001) J. Chem. Phys. , vol.114 , pp. 561-569
    • Bratko, D.1    Blanch, H.W.2
  • 27
    • 67649101377 scopus 로고    scopus 로고
    • Generic Coarse-Grained Model for Protein Folding and Aggregation
    • Bereau, T.; Deserno, M. Generic Coarse-Grained Model for Protein Folding and Aggregation J. Chem. Phys. 2009, 130, 235106 10.1063/1.3152842
    • (2009) J. Chem. Phys. , vol.130 , pp. 235106
    • Bereau, T.1    Deserno, M.2
  • 28
    • 84882330872 scopus 로고    scopus 로고
    • Efficient Determination of Protein-Protein Standard Binding Free Energies from First Principles
    • Gumbart, J. C.; Roux, B.; Chipot, C. Efficient Determination of Protein-Protein Standard Binding Free Energies from First Principles J. Chem. Theory Comput. 2013, 9, 3789-3798 10.1021/ct400273t
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 3789-3798
    • Gumbart, J.C.1    Roux, B.2    Chipot, C.3
  • 29
    • 84872165531 scopus 로고    scopus 로고
    • Standard Binding Free Energies from Computer Simulations: What Is the Best Strategy?
    • Gumbart, J. C.; Roux, B.; Chipot, C. Standard Binding Free Energies from Computer Simulations: What Is the Best Strategy? J. Chem. Theory Comput. 2013, 9, 794-802 10.1021/ct3008099
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 794-802
    • Gumbart, J.C.1    Roux, B.2    Chipot, C.3
  • 30
    • 77956154559 scopus 로고    scopus 로고
    • Downhill Binding Energy Surface of the Barnase-Barstar Complex
    • Wang, L.; Siu, S. W. I.; Gu, W.; Helms, V. Downhill Binding Energy Surface of the Barnase-Barstar Complex Biopolymers 2010, 93, 977-985 10.1002/bip.21507
    • (2010) Biopolymers , vol.93 , pp. 977-985
    • Wang, L.1    Siu, S.W.I.2    Gu, W.3    Helms, V.4
  • 31
    • 18744372751 scopus 로고    scopus 로고
    • Calculation of Absolute Protein-Ligand Binding Free Energy from Computer Simulations
    • Woo, H. J.; Roux, B. Calculation of Absolute Protein-Ligand Binding Free Energy from Computer Simulations Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 6825-6830 10.1073/pnas.0409005102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6825-6830
    • Woo, H.J.1    Roux, B.2
  • 32
    • 84931477990 scopus 로고    scopus 로고
    • Efficient Calculation of Relative Binding Free Energies by Umbrella Sampling Perturbation
    • Zeller, F.; Zacharias, M. Efficient Calculation of Relative Binding Free Energies by Umbrella Sampling Perturbation J. Comput. Chem. 2014, 35, 2256-2262 10.1002/jcc.23744
    • (2014) J. Comput. Chem. , vol.35 , pp. 2256-2262
    • Zeller, F.1    Zacharias, M.2
  • 33
    • 84986497803 scopus 로고
    • Multidimensional Free-Energy Calculations Using the Weighted Histogram Analysis Method
    • Kumar, S.; Rosenberg, J. M.; Bouzida, D.; Swendsen, R. H.; Kollman, P. A. Multidimensional Free-Energy Calculations Using the Weighted Histogram Analysis Method J. Comput. Chem. 1995, 16, 1339-1350 10.1002/jcc.540161104
    • (1995) J. Comput. Chem. , vol.16 , pp. 1339-1350
    • Kumar, S.1    Rosenberg, J.M.2    Bouzida, D.3    Swendsen, R.H.4    Kollman, P.A.5
  • 34
    • 0032960853 scopus 로고    scopus 로고
    • Self-Consistent Estimation of Inter-Residue Protein Contact Energies Based on an Equilibrium Mixture Approximation of Residues
    • Miyazawa, S.; Jernigan, R. L. Self-Consistent Estimation of Inter-Residue Protein Contact Energies Based on an Equilibrium Mixture Approximation of Residues Proteins: Struct., Funct., Genet. 1999, 34, 49-68 10.1002/(SICI)1097-0134(19990101)34:1<49::AID-PROT5>3.3.CO;2-C
    • (1999) Proteins: Struct., Funct., Genet. , vol.34 , pp. 49-68
    • Miyazawa, S.1    Jernigan, R.L.2
  • 35
    • 0029909384 scopus 로고    scopus 로고
    • An Iterative Method for Extracting Energy-like Quantities from Protein Structures
    • Thomas, P. D.; Dill, K. A. An Iterative Method for Extracting Energy-like Quantities from Protein Structures Proc. Natl. Acad. Sci. U. S. A. 1996, 93, 11628-11633 10.1073/pnas.93.21.11628
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11628-11633
    • Thomas, P.D.1    Dill, K.A.2
  • 36
    • 34247179107 scopus 로고    scopus 로고
    • Continuum Theory of Polymer Crystallization
    • Kundagrami, A.; Muthukumar, M. Continuum Theory of Polymer Crystallization J. Chem. Phys. 2007, 126, 144901 10.1063/1.2713380
    • (2007) J. Chem. Phys. , vol.126 , pp. 144901
    • Kundagrami, A.1    Muthukumar, M.2
  • 37
    • 84861706182 scopus 로고    scopus 로고
    • Langevin Dynamics Simulation of Polymer-Assisted Virus-like Assembly
    • Mahalik, J. P.; Muthukumar, M. Langevin Dynamics Simulation of Polymer-Assisted Virus-like Assembly J. Chem. Phys. 2012, 136, 135101 10.1063/1.3698408
    • (2012) J. Chem. Phys. , vol.136 , pp. 135101
    • Mahalik, J.P.1    Muthukumar, M.2
  • 38
    • 84889604825 scopus 로고    scopus 로고
    • Biogenesis of a Bacterial Organelle: The Carboxysome Assembly Pathway
    • Cameron, J. C.; Wilson, S. C.; Bernstein, S. L.; Kerfeld, C. A. Biogenesis of a Bacterial Organelle: The Carboxysome Assembly Pathway Cell 2013, 155, 1131-1140 10.1016/j.cell.2013.10.044
    • (2013) Cell , vol.155 , pp. 1131-1140
    • Cameron, J.C.1    Wilson, S.C.2    Bernstein, S.L.3    Kerfeld, C.A.4
  • 39
    • 0036786867 scopus 로고    scopus 로고
    • Weak Protein-Protein Interactions Are Sufficient to Drive Assembly of Hepatitis B Virus Capsids
    • Ceres, P.; Zlotnick, A. Weak Protein-Protein Interactions Are Sufficient to Drive Assembly of Hepatitis B Virus Capsids Biochemistry 2002, 41, 11525-11531 10.1021/bi0261645
    • (2002) Biochemistry , vol.41 , pp. 11525-11531
    • Ceres, P.1    Zlotnick, A.2
  • 40
    • 0035997081 scopus 로고    scopus 로고
    • Model-Based Analysis of Assembly Kinetics for Virus Capsids or Other Spherical Polymers
    • Endres, D.; Zlotnick, A. Model-Based Analysis of Assembly Kinetics for Virus Capsids or Other Spherical Polymers Biophys. J. 2002, 83, 1217-1230 10.1016/S0006-3495(02)75245-4
    • (2002) Biophys. J. , vol.83 , pp. 1217-1230
    • Endres, D.1    Zlotnick, A.2
  • 41
    • 84903731786 scopus 로고    scopus 로고
    • Modeling Viral Capsid Assembly
    • Hagan, M. F. Modeling Viral Capsid Assembly Adv. Chem. Phys. 2014, 155, 1-67 10.1002/9781118755815.ch01
    • (2014) Adv. Chem. Phys. , vol.155 , pp. 1-67
    • Hagan, M.F.1
  • 42
    • 33745787907 scopus 로고    scopus 로고
    • Dynamic Pathways for Viral Capsid Assembly
    • Hagan, M. F.; Chandler, D. Dynamic Pathways for Viral Capsid Assembly Biophys. J. 2006, 91, 42-54 10.1529/biophysj.105.076851
    • (2006) Biophys. J. , vol.91 , pp. 42-54
    • Hagan, M.F.1    Chandler, D.2
  • 43
    • 80052957030 scopus 로고    scopus 로고
    • Mechanisms of Kinetic Trapping in Self-Assembly and Phase Transformation
    • Hagan, M. F.; Elrad, O. M.; Jack, R. L. Mechanisms of Kinetic Trapping in Self-Assembly and Phase Transformation J. Chem. Phys. 2011, 135, 104115 10.1063/1.3635775
    • (2011) J. Chem. Phys. , vol.135 , pp. 104115
    • Hagan, M.F.1    Elrad, O.M.2    Jack, R.L.3
  • 44
    • 0034715825 scopus 로고    scopus 로고
    • Mechanism of Capsid Assembly for an Icosahedral Plant Virus
    • Zlotnick, A.; Aldrich, R.; Johnson, J. M.; Ceres, P.; Young, M. J. Mechanism of Capsid Assembly for an Icosahedral Plant Virus Virology 2000, 277, 450-456 10.1006/viro.2000.0619
    • (2000) Virology , vol.277 , pp. 450-456
    • Zlotnick, A.1    Aldrich, R.2    Johnson, J.M.3    Ceres, P.4    Young, M.J.5
  • 45
    • 0033517792 scopus 로고    scopus 로고
    • A Theoretical Model Successfully Identifies Features of Hepatitis B Virus Capsid Assembly
    • Zlotnick, A.; Johnson, J. M.; Wingfield, P. W.; Stahl, S. J.; Endres, D. A Theoretical Model Successfully Identifies Features of Hepatitis B Virus Capsid Assembly Biochemistry 1999, 38, 14644-14652 10.1021/bi991611a
    • (1999) Biochemistry , vol.38 , pp. 14644-14652
    • Zlotnick, A.1    Johnson, J.M.2    Wingfield, P.W.3    Stahl, S.J.4    Endres, D.5
  • 46
    • 84976615324 scopus 로고    scopus 로고
    • http://agknapp.chemie.fu-berlin.de/karlsberg/.
  • 47
    • 0029878720 scopus 로고    scopus 로고
    • VMD - Visual Molecular Dynamics
    • Humphrey, W.; Dalke, A.; Schulten, K. VMD-Visual Molecular Dynamics J. Mol. Graphics 1996, 14, 33-38 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graphics , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 48
    • 84976625526 scopus 로고    scopus 로고
    • http://www.ks.uiuc.edu/Research/vmd/.
  • 50
    • 84908350120 scopus 로고    scopus 로고
    • A Taxonomy of Bacterial Microcompartment Loci Constructed by a Novel Scoring Method
    • Axen, S. D.; Erbilgin, O.; Kerfeld, C. A. A Taxonomy of Bacterial Microcompartment Loci Constructed by a Novel Scoring Method PLoS Comput. Biol. 2014, 10, e1003898 10.1371/journal.pcbi.1003898
    • (2014) PLoS Comput. Biol. , vol.10 , pp. e1003898
    • Axen, S.D.1    Erbilgin, O.2    Kerfeld, C.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.