메뉴 건너뛰기




Volumn 106, Issue 6, 2014, Pages 1338-1348

Elastic properties and heterogeneous stiffness of the Phi29 motor connector channel

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CAPSID PROTEIN; PORTAL PROTEIN, BACTERIOPHAGE PHI29; PROTEIN BINDING; VIRUS DNA;

EID: 84896522348     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.01.028     Document Type: Article
Times cited : (20)

References (80)
  • 2
    • 16844376846 scopus 로고    scopus 로고
    • Bacterial virus φ29 DNA-packaging motor and its potential applications in gene therapy and nanotechnology
    • P. Guo Bacterial virus φ29 DNA-packaging motor and its potential applications in gene therapy and nanotechnology Methods Mol. Biol. 300 2005 285 324
    • (2005) Methods Mol. Biol. , vol.300 , pp. 285-324
    • Guo, P.1
  • 3
    • 0023651217 scopus 로고
    • Characterization of the small RNA of the bacteriophage φ29 DNA packaging machine
    • P.X. Guo, and S. Bailey D. Anderson Characterization of the small RNA of the bacteriophage φ29 DNA packaging machine Nucleic Acids Res. 15 1987 7081 7090
    • (1987) Nucleic Acids Res. , vol.15 , pp. 7081-7090
    • Guo, P.X.1    Bailey, S.2    Anderson, D.3
  • 4
    • 0023225629 scopus 로고
    • A small viral RNA is required for in vitro packaging of bacteriophage 29 DNA
    • P.X. Guo, S. Erickson, and D. Anderson A small viral RNA is required for in vitro packaging of bacteriophage φ29 DNA Science 236 1987 690 694 (Pubitemid 17076855)
    • (1987) Science , vol.236 , Issue.4802 , pp. 690-694
    • Guo, P.1    Erickson, S.2    Anderson, D.3
  • 5
    • 31344436408 scopus 로고    scopus 로고
    • Interaction of gp16 with pRNA and DNA for genome packaging by the motor of bacterial virus phi29
    • DOI 10.1016/j.jmb.2005.10.045, PII S0022283605012891
    • T.J. Lee, and P. Guo Interaction of gp16 with pRNA and DNA for genome packaging by the motor of bacterial virus φ29 J. Mol. Biol. 356 2006 589 599 (Pubitemid 43139322)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.3 , pp. 589-599
    • Lee, T.-J.1    Guo, P.2
  • 6
    • 0028000731 scopus 로고
    • Structure of viral connectors and their function in bacteriophage assembly and DNA packaging
    • J.M. Valpuesta, and J.L. Carrascosa Structure of viral connectors and their function in bacteriophage assembly and DNA packaging Q. Rev. Biophys. 27 1994 107 155 (Pubitemid 24246113)
    • (1994) Quarterly Reviews of Biophysics , vol.27 , Issue.2 , pp. 107-155
    • Valpuesta, J.M.1    Carrascosa, J.L.2
  • 7
    • 78651295835 scopus 로고    scopus 로고
    • EMDataBank.org: Unified data resource for CryoEM
    • C.L. Lawson, and M.L. Baker W. Chiu EMDataBank.org: unified data resource for CryoEM Nucleic Acids Res. 39 Database issue 2011 D456 D464
    • (2011) Nucleic Acids Res. , vol.39 , Issue.DATABASE ISS.
    • Lawson, C.L.1    Baker, M.L.2    Chiu, W.3
  • 8
    • 17044395121 scopus 로고    scopus 로고
    • Conservation of the capsid structure in tailed dsDNA bacteriophages: The pseudoatomic structure of φ29
    • M.C. Morais, and K.H. Choi M.G. Rossmann Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of φ29 Mol. Cell 18 2005 149 159
    • (2005) Mol. Cell , vol.18 , pp. 149-159
    • Morais, M.C.1    Choi, K.H.2    Rossmann, M.G.3
  • 10
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage 29 portal motor can package DNA against a large internal force
    • DOI 10.1038/35099581
    • D.E. Smith, and S.J. Tans C. Bustamante The bacteriophage straight φ29 portal motor can package DNA against a large internal force Nature 413 2001 748 752 (Pubitemid 33009954)
    • (2001) Nature , vol.413 , Issue.6857 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 11
    • 0042172858 scopus 로고    scopus 로고
    • Bacterial virus phi29 pRNA as a hammerhead ribozyme escort to destroy hepatitis B virus
    • DOI 10.1038/sj.gt.3302002
    • S. Hoeprich, and Q. Zhou P. Guo Bacterial virus φ29 pRNA as a hammerhead ribozyme escort to destroy hepatitis B virus Gene Ther. 10 2003 1258 1267 (Pubitemid 36934728)
    • (2003) Gene Therapy , vol.10 , Issue.15 , pp. 1258-1267
    • Heoprich, S.1    Zhou, Q.2    Guo, S.3    Shu, D.4    Qi, G.5    Wang, Y.6    Guo, P.7
  • 12
    • 77953811389 scopus 로고    scopus 로고
    • Mechanochemistry of a viral DNA packaging motor
    • J. Yu, and J. Moffitt G. Oster Mechanochemistry of a viral DNA packaging motor J. Mol. Biol. 400 2010 186 203
    • (2010) J. Mol. Biol. , vol.400 , pp. 186-203
    • Yu, J.1    Moffitt, J.2    Oster, G.3
  • 13
    • 58749087869 scopus 로고    scopus 로고
    • Intersubunit coordination in a homomeric ring ATPase
    • J.R. Moffitt, and Y.R. Chemla C. Bustamante Intersubunit coordination in a homomeric ring ATPase Nature 457 2009 446 450
    • (2009) Nature , vol.457 , pp. 446-450
    • Moffitt, J.R.1    Chemla, Y.R.2    Bustamante, C.3
  • 14
    • 37749051185 scopus 로고    scopus 로고
    • Portal motor velocity and internal force resisting viral DNA packaging in bacteriophage φ29
    • J.P. Rickgauer, and D.N. Fuller D.E. Smith Portal motor velocity and internal force resisting viral DNA packaging in bacteriophage φ29 Biophys. J. 94 2008 159 167
    • (2008) Biophys. J. , vol.94 , pp. 159-167
    • Rickgauer, J.P.1    Fuller, D.N.2    Smith, D.E.3
  • 16
    • 79951816920 scopus 로고    scopus 로고
    • Built-in mechanical stress in viral shells
    • C. Carrasco, and A. Luque P.J. de Pablo Built-in mechanical stress in viral shells Biophys. J. 100 2011 1100 1108
    • (2011) Biophys. J. , vol.100 , pp. 1100-1108
    • Carrasco, C.1    Luque, A.2    De Pablo, P.J.3
  • 19
    • 33947213307 scopus 로고    scopus 로고
    • Experimental test of connector rotation during DNA packaging into bacteriophage φ29 capsids
    • T. Hugel, and J. Michaelis C. Bustamante Experimental test of connector rotation during DNA packaging into bacteriophage φ29 capsids PLoS Biol. 5 2007 e59
    • (2007) PLoS Biol. , vol.5 , pp. 59
    • Hugel, T.1    Michaelis, J.2    Bustamante, C.3
  • 20
    • 70349665213 scopus 로고    scopus 로고
    • Substrate interactions and promiscuity in a viral DNA packaging motor
    • K. Aathavan, and A.T. Politzer C. Bustamante Substrate interactions and promiscuity in a viral DNA packaging motor Nature 461 2009 669 673
    • (2009) Nature , vol.461 , pp. 669-673
    • Aathavan, K.1    Politzer, A.T.2    Bustamante, C.3
  • 21
    • 84878292282 scopus 로고    scopus 로고
    • Mechanism of one-way traffic of hexameric φ29 DNA packaging motor with four electropositive relaying layers facilitating antiparallel revolution
    • Z. Zhao, and E. Khisamutdinov P. Guo Mechanism of one-way traffic of hexameric φ29 DNA packaging motor with four electropositive relaying layers facilitating antiparallel revolution ACS Nano 7 2013 4082 4092
    • (2013) ACS Nano , vol.7 , pp. 4082-4092
    • Zhao, Z.1    Khisamutdinov, E.2    Guo, P.3
  • 22
    • 84880948085 scopus 로고    scopus 로고
    • Ultrastable pRNA hexameric ring gearing hexameric φ29 DNA-packaging motor by revolving without rotating and coiling
    • C. Schwartz, and P. Guo Ultrastable pRNA hexameric ring gearing hexameric φ29 DNA-packaging motor by revolving without rotating and coiling Curr. Opin. Biotechnol. 24 2013 581 590
    • (2013) Curr. Opin. Biotechnol. , vol.24 , pp. 581-590
    • Schwartz, C.1    Guo, P.2
  • 23
    • 84879787373 scopus 로고    scopus 로고
    • Revolution rather than rotation of AAA+ hexameric φ29 nanomotor for viral dsDNA packaging without coiling
    • C. Schwartz, and G.M. De Donatis P. Guo Revolution rather than rotation of AAA+ hexameric φ29 nanomotor for viral dsDNA packaging without coiling Virology 443 2013 28 39
    • (2013) Virology , vol.443 , pp. 28-39
    • Schwartz, C.1    De Donatis, G.M.2    Guo, P.3
  • 24
    • 84879785627 scopus 로고    scopus 로고
    • The ATPase of the φ29 DNA packaging motor is a member of the hexameric AAA+ superfamily
    • C. Schwartz, and G.M. De Donatis P. Guo The ATPase of the φ29 DNA packaging motor is a member of the hexameric AAA+ superfamily Virology 443 2013 20 27
    • (2013) Virology , vol.443 , pp. 20-27
    • Schwartz, C.1    De Donatis, G.M.2    Guo, P.3
  • 25
    • 84862878463 scopus 로고    scopus 로고
    • Chapt. 9. "push through one-way valve" mechanism of viral DNA packaging
    • Małgorzata, S. Wacław, Academic Press New York
    • H. Zhang, and C. Schwartz P. Guo Chapt. 9. "Push through one-way valve" mechanism of viral DNA packaging Ł. Małgorzata, S. Wacław, Advances in Virus Research 2012 Academic Press New York 415 465
    • (2012) Advances in Virus Research , pp. 415-465
    • Zhang, H.1    Schwartz, C.2    Guo, P.3
  • 26
    • 84855423787 scopus 로고    scopus 로고
    • Role of channel lysines and the "push through a one-way valve" mechanism of the viral DNA packaging motor
    • H. Fang, and P. Jing P. Guo Role of channel lysines and the "push through a one-way valve" mechanism of the viral DNA packaging motor Biophys. J. 102 2012 127 135
    • (2012) Biophys. J. , vol.102 , pp. 127-135
    • Fang, H.1    Jing, P.2    Guo, P.3
  • 27
    • 77956448643 scopus 로고    scopus 로고
    • One-way traffic of a viral motor channel for double-stranded DNA translocation
    • P. Jing, and F. Haque P. Guo One-way traffic of a viral motor channel for double-stranded DNA translocation Nano Lett. 10 2010 3620 3627
    • (2010) Nano Lett. , vol.10 , pp. 3620-3627
    • Jing, P.1    Haque, F.2    Guo, P.3
  • 28
    • 0030059225 scopus 로고    scopus 로고
    • Ligand binding: Molecular mechanics calculation of the streptavidin-biotin rupture force
    • H. Grubmüller, B. Heymann, and P. Tavan Ligand binding: molecular mechanics calculation of the streptavidin-biotin rupture force Science 271 1996 997 999 (Pubitemid 26066398)
    • (1996) Science , vol.271 , Issue.5251 , pp. 997-999
    • Grubmuller, H.1    Heymann, B.2    Tavan, P.3
  • 29
    • 79955901803 scopus 로고    scopus 로고
    • Keep it flexible: Driving macromolecular rotary motions in atomistic simulations with GROMACS
    • C. Kutzner, J. Czub, and H. Grubmüller Keep it flexible: driving macromolecular rotary motions in atomistic simulations with GROMACS J. Chem. Theory Comput. 7 2011 1381 1393
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 1381-1393
    • Kutzner, C.1    Czub, J.2    Grubmüller, H.3
  • 30
    • 62649155309 scopus 로고    scopus 로고
    • Mechanical properties of the icosahedral shell of Southern bean mosaic virus: A molecular dynamics study
    • M. Zink, and H. Grubmüller Mechanical properties of the icosahedral shell of Southern bean mosaic virus: a molecular dynamics study Biophys. J. 96 2009 1350 1363
    • (2009) Biophys. J. , vol.96 , pp. 1350-1363
    • Zink, M.1    Grubmüller, H.2
  • 32
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, and C. Kutzner E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Lindahl, E.3
  • 34
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • W.L. Jorgensen, and J. Chandrasekhar M.L. Klein Comparison of simple potential functions for simulating liquid water J. Chem. Phys. 79 1983 926 935
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 35
    • 33846823909 scopus 로고
    • Particle mesh Ewald - An N.log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald - an N.log(N) method for Ewald sums in large systems j. Chem. Phys. 98 1993 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 36
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • G. Bussi, D. Donadio, and M. Parrinello Canonical sampling through velocity rescaling J. Chem. Phys. 126 2007 014101
    • (2007) J. Chem. Phys. , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 37
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • H.J.C. Berendsen, and J.P.M. Postma J.R. Haak Molecular dynamics with coupling to an external bath J. Chem. Phys. 81 1984 3684 3690
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Haak, J.R.3
  • 38
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • S. Nose, and M.L. Klein Constant pressure molecular dynamics for molecular systems Mol. Phys. 50 1983 1055 1076
    • (1983) Mol. Phys. , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.L.2
  • 39
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • B. Hess P-LINCS: A parallel linear constraint solver for molecular simulation J. Chem. Theory Comput. 4 2008 116 122
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 42
    • 78651282170 scopus 로고    scopus 로고
    • G-WHAM-A free weighted histogram analysis implementation including robust error and autocorrelation estimates
    • J.S. Hub, B.L. de Groot, and D. van der Spoel G-WHAM-A free weighted histogram analysis implementation including robust error and autocorrelation estimates J. Chem. Theory Comput. 6 2010 3713 3720
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 3713-3720
    • Hub, J.S.1    De Groot, B.L.2    Van Der Spoel, D.3
  • 43
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method
    • S. Kumar, and D. Bouzida J.M. Rosenberg The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method J. Comput. Chem. 13 1992 1011 1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Rosenberg, J.M.3
  • 44
    • 0029633155 scopus 로고
    • The calculation of the potential of mean force using computer-simulations
    • B. Roux The calculation of the potential of mean force using computer-simulations Comput. Phys. Commun. 91 1995 275 282
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 275-282
    • Roux, B.1
  • 45
    • 0004253046 scopus 로고    scopus 로고
    • Brooks/Cole-Thomson/Cengage Learning Stamford, CT
    • J.M. Gere Mechanics of Materials 2004 Brooks/Cole-Thomson/Cengage Learning Stamford, CT 78 83
    • (2004) Mechanics of Materials , pp. 78-83
    • Gere, J.M.1
  • 46
    • 84986483798 scopus 로고
    • The double cubic lattice method - Efficient approaches to numerical-integration of surface-area and volume and to dot surface contouring of molecular assemblies
    • F. Eisenhaber, and P. Lijnzaad M. Scharf The double cubic lattice method - efficient approaches to numerical-integration of surface-area and volume and to dot surface contouring of molecular assemblies J. Comput. Chem. 16 1995 273 284
    • (1995) J. Comput. Chem. , vol.16 , pp. 273-284
    • Eisenhaber, F.1    Lijnzaad, P.2    Scharf, M.3
  • 49
    • 0342288072 scopus 로고    scopus 로고
    • Mechanical properties of single-brin silkworm silk
    • DOI 10.1002/(SICI)1097-4628(20000307)75:10<1270::AID-APP8>3.0.CO;2- C
    • J. Perez-Rigueiro, and C. Viney M. Elices Mechanical properties of single-brin silkworm silk J. Appl. Polym. Sci. 75 2000 1270 1277 (Pubitemid 32211546)
    • (2000) Journal of Applied Polymer Science , vol.75 , Issue.10 , pp. 1270-1277
    • Perez-Rigueiro, J.1    Viney, C.2    Llorca, J.3    Elices, M.4
  • 50
    • 0028480541 scopus 로고
    • Mechanical and thermal properties of dragline silk from the spider Nephila clavipes
    • P.M. Cunniff, and S.A. Fossey D.L. Vezie Mechanical and thermal properties of dragline silk from the spider Nephila clavipes Polym. Adv. Technol. 5 1994 401 410
    • (1994) Polym. Adv. Technol. , vol.5 , pp. 401-410
    • Cunniff, P.M.1    Fossey, S.A.2    Vezie, D.L.3
  • 53
    • 34547130847 scopus 로고    scopus 로고
    • Structural rearrangements between portal protein subunits are essential for viral DNA translocation
    • DOI 10.1074/jbc.M701808200
    • A. Cuervo, and M.C. Vaney L. Oliveira Structural rearrangements between portal protein subunits are essential for viral DNA translocation J. Biol. Chem. 282 2007 18907 18913 (Pubitemid 47100132)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.26 , pp. 18907-18913
    • Cuervo, A.1    Vaney, M.-C.2    Antson, A.A.3    Tavares, P.4    Oliveira, L.5
  • 55
    • 66649092587 scopus 로고    scopus 로고
    • Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating
    • S. Lhuillier, and M. Gallopin S. Zinn-Justin Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating Proc. Natl. Acad. Sci. USA 106 2009 8507 8512
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8507-8512
    • Lhuillier, S.1    Gallopin, M.2    Zinn-Justin, S.3
  • 56
    • 85027920272 scopus 로고    scopus 로고
    • Three-dimensional structure of a viral genome-delivery portal vertex
    • A.S. Olia, and P.E. Prevelige Jr. G. Cingolani Three-dimensional structure of a viral genome-delivery portal vertex Nat. Struct. Mol. Biol. 18 2011 597 603
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 597-603
    • Olia, A.S.1    Prevelige, Jr.P.E.2    Cingolani, G.3
  • 57
    • 80052206993 scopus 로고    scopus 로고
    • A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries
    • D. Veesler, and C. Cambillau A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries Microbiol. Mol. Biol. Rev. 75 2011 423 433
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 423-433
    • Veesler, D.1    Cambillau, C.2
  • 58
    • 63049104932 scopus 로고    scopus 로고
    • The elaborate structure of spider silk: Structure and function of a natural high performance fiber
    • L. Römer, and T. Scheibel The elaborate structure of spider silk: structure and function of a natural high performance fiber Prion 2 2008 154 161
    • (2008) Prion , vol.2 , pp. 154-161
    • Römer, L.1    Scheibel, T.2
  • 59
    • 33747192713 scopus 로고
    • Control and design principles in biological mineralization
    • L. Addadi, and S. Weiner Control and design principles in biological mineralization Angew. Chem. Int. Ed. Engl. 31 1992 153 169
    • (1992) Angew. Chem. Int. Ed. Engl. , vol.31 , pp. 153-169
    • Addadi, L.1    Weiner, S.2
  • 60
    • 77956900242 scopus 로고    scopus 로고
    • Mineralized structures in nature: Examples and inspirations for the design of new composite materials and biomaterials
    • G.M. Luz, and J.F. Mano Mineralized structures in nature: examples and inspirations for the design of new composite materials and biomaterials Compos. Sci. Technol. 70 2010 1777 1788
    • (2010) Compos. Sci. Technol. , vol.70 , pp. 1777-1788
    • Luz, G.M.1    Mano, J.F.2
  • 61
    • 79958703404 scopus 로고    scopus 로고
    • Role of φ29 connector channel loops in late-stage DNA packaging
    • S. Grimes, and S. Ma P.J. Jardine Role of φ29 connector channel loops in late-stage DNA packaging J. Mol. Biol. 410 2011 50 59
    • (2011) J. Mol. Biol. , vol.410 , pp. 50-59
    • Grimes, S.1    Ma, S.2    Jardine, P.J.3
  • 62
    • 0028929583 scopus 로고
    • Free energy balance in protein folding
    • B. Honig, and A.S. Yang Free energy balance in protein folding Adv. Protein Chem. 46 1995 27 58
    • (1995) Adv. Protein Chem. , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.S.2
  • 63
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • D. Eisenberg, and A.D. McLachlan Solvation energy in protein folding and binding Nature 319 1986 199 203 (Pubitemid 16128783)
    • (1986) Nature , vol.319 , Issue.6050 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 64
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • DOI 10.1021/bi00483a001
    • K.A. Dill Dominant forces in protein folding Biochemistry 29 1990 7133 7155 (Pubitemid 20230041)
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 65
    • 0030056418 scopus 로고    scopus 로고
    • Hydrophobic regions on protein surfaces. Derivation of the solvation energy from their area distribution in crystallographic protein structures
    • F. Eisenhaber Hydrophobic regions on protein surfaces. Derivation of the solvation energy from their area distribution in crystallographic protein structures Protein Sci. 5 1996 1676 1686 (Pubitemid 26257230)
    • (1996) Protein Science , vol.5 , Issue.8 , pp. 1676-1686
    • Eisenhaber, F.1
  • 66
    • 33847217662 scopus 로고    scopus 로고
    • Fluctuations of primary ubiquitin folding intermediates in a force clamp
    • F. Gräter, and H. Grubmüller Fluctuations of primary ubiquitin folding intermediates in a force clamp J. Struct. Biol. 157 2007 557 569
    • (2007) J. Struct. Biol. , vol.157 , pp. 557-569
    • Gräter, F.1    Grubmüller, H.2
  • 67
    • 1542513548 scopus 로고    scopus 로고
    • Force-Clamp Spectroscopy Monitors the Folding Trajectory of a Single Protein
    • DOI 10.1126/science.1092497
    • J.M. Fernandez, and H. Li Force-clamp spectroscopy monitors the folding trajectory of a single protein Science 303 2004 1674 1678 (Pubitemid 38338326)
    • (2004) Science , vol.303 , Issue.5664 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 68
    • 77956544822 scopus 로고    scopus 로고
    • An unusual hydrophobic core confers extreme flexibility to HEAT repeat proteins
    • C. Kappel, and U. Zachariae H. Grubmüller An unusual hydrophobic core confers extreme flexibility to HEAT repeat proteins Biophys. J. 99 2010 1596 1603
    • (2010) Biophys. J. , vol.99 , pp. 1596-1603
    • Kappel, C.1    Zachariae, U.2    Grubmüller, H.3
  • 69
    • 84866392763 scopus 로고    scopus 로고
    • Universal relaxation governs the nonequilibrium elasticity of biomolecules
    • C. Kappel, and N. Dölker H. Grubmüller Universal relaxation governs the nonequilibrium elasticity of biomolecules Phys. Rev. Lett. 109 2012 118304
    • (2012) Phys. Rev. Lett. , vol.109 , pp. 118304
    • Kappel, C.1    Dölker, N.2    Grubmüller, H.3
  • 70
    • 77249145890 scopus 로고    scopus 로고
    • Primary changes of the mechanical properties of Southern Bean Mosaic Virus upon calcium removal
    • M. Zink, and H. Grubmüller Primary changes of the mechanical properties of Southern Bean Mosaic Virus upon calcium removal Biophys. J. 98 2010 687 695
    • (2010) Biophys. J. , vol.98 , pp. 687-695
    • Zink, M.1    Grubmüller, H.2
  • 72
    • 0034127361 scopus 로고    scopus 로고
    • Collective protein dynamics in relation to function
    • DOI 10.1016/S0959-440X(00)00061-0
    • H.J. Berendsen, and S. Hayward Collective protein dynamics in relation to function Curr. Opin. Struct. Biol. 10 2000 165 169 (Pubitemid 30198942)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.2 , pp. 165-169
    • Berendsen, H.J.1    Hayward, S.2
  • 73
    • 50149097363 scopus 로고    scopus 로고
    • Comparative protein structure modeling using MODELLER
    • 10.1002/0471140864.ps0209s50 Chapter 2:Unit 2.9
    • N. Eswar, and B. Webb A. Sali Comparative protein structure modeling using MODELLER Curr. Protoc. Protein. Sci. 2007 10.1002/0471140864.ps0209s50 Chapter 2:Unit 2.9
    • (2007) Curr. Protoc. Protein. Sci.
    • Eswar, N.1    Webb, B.2    Sali, A.3
  • 74
    • 33747863016 scopus 로고    scopus 로고
    • ArchPRED: A template based loop structure prediction server
    • N. Fernandez-Fuentes, J. Zhai, and A. Fiser ArchPRED: a template based loop structure prediction server Nucleic Acids Res. 34 Web Server issue 2006 W173 W176
    • (2006) Nucleic Acids Res. , vol.34 , Issue.WEB SERVER ISS.
    • Fernandez-Fuentes, N.1    Zhai, J.2    Fiser, A.3
  • 75
    • 0000577041 scopus 로고
    • Large-amplitude nonlinear motions in proteins
    • A.E. García Large-amplitude nonlinear motions in proteins Phys. Rev. Lett. 68 1992 2696 2699
    • (1992) Phys. Rev. Lett. , vol.68 , pp. 2696-2699
    • García, A.E.1
  • 76
    • 0027732618 scopus 로고
    • Effect of solvent on collective motions in globular protein
    • DOI 10.1006/jmbi.1993.1671
    • S. Hayward, and A. Kitao N. Go Effect of solvent on collective motions in globular protein J. Mol. Biol. 234 1993 1207 1217 (Pubitemid 24027248)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.4 , pp. 1207-1217
    • Hayward, S.1    Kitao, A.2    Hirata, F.3    Go, N.4
  • 78
    • 0000998079 scopus 로고
    • The effects of solvent on the conformation and the collective motions of protein: Normal mode analysis and molecular dynamics simulations of melittin in water and in vacuum
    • A. Kitao, F. Hirata, and N. Gō The effects of solvent on the conformation and the collective motions of protein: normal mode analysis and molecular dynamics simulations of melittin in water and in vacuum Chem. Phys. 158 1991 447 472
    • (1991) Chem. Phys. , vol.158 , pp. 447-472
    • Kitao, A.1    Hirata, F.2    Go, N.3
  • 79
    • 0001444487 scopus 로고    scopus 로고
    • Modeling unusual nucleic acid structures
    • American Chemical Society Washington, DC
    • J. Macke Thomas, and A. Case David Modeling unusual nucleic acid structures Molecular Modeling of Nucleic Acids 1997 American Chemical Society Washington, DC 379 393
    • (1997) Molecular Modeling of Nucleic Acids , pp. 379-393
    • Macke Thomas, J.1    Case David, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.