메뉴 건너뛰기




Volumn 34, Issue , 2012, Pages 28-37

The harmonic analysis of cylindrically symmetric proteins: A comparison of Dronpa and a DNA sliding clamp

Author keywords

Normal mode analysis; Protein topology; Symmetric proteins

Indexed keywords

BREATHING MOTIONS; CORRELATED MOTIONS; CORRELATION DIAGRAMS; CYLINDRICAL ROD; CYLINDRICAL SYMMETRY; ELASTIC BEHAVIOR; ELASTIC MODES; ELASTIC NETWORK MODELS; LOW FREQUENCY; MOLECULAR DYNAMICS SIMULATIONS; NORMAL MODE ANALYSIS; NORMAL MODES; PRINCIPAL COMPONENTS; PROTEIN TOPOLOGY; STANDARD FORCE FIELD;

EID: 84856456583     PISSN: 10933263     EISSN: 18734243     Source Type: Journal    
DOI: 10.1016/j.jmgm.2011.12.005     Document Type: Article
Times cited : (12)

References (63)
  • 3
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • X-P. Kong, R. Onrust, M. O'Donnell, and J. Kuriyan Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp Cell 69 1992 425 437
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.-P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 4
    • 0031045565 scopus 로고    scopus 로고
    • PCNA: Structure functions and interactions
    • Z. Kelman PCNA: structure functions and interactions Oncogene 14 1997 629 640
    • (1997) Oncogene , vol.14 , pp. 629-640
    • Kelman, Z.1
  • 6
    • 0037142745 scopus 로고    scopus 로고
    • Green fluorescent proteins: Empirical force field for the neutral and deprotonated forms of the chromophore. Molecular dynamics simulations of the wild type and S65T mutant
    • DOI 10.1021/jp014476w
    • N. Reuter, H. Lin, and W. Thiel Green fluorescent proteins: empirical force field for the neutral and deprotonated forms of the chromophore. Molecular dynamics simulations of the wild type and S65T mutant J. Phys. Chem. B 106 2002 6310 6321 (Pubitemid 35281815)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.24 , pp. 6310-6321
    • Reuter, N.1    Lin, H.2    Thiel, W.3
  • 7
    • 0038300350 scopus 로고    scopus 로고
    • Molecular dynamics simulations of enhanced Green Fluorescent Proteins: Effects of F64L, S65T and T203Y mutations on the ground-state proton equilibria
    • DOI 10.1002/prot.10335
    • R. Nifosi, and V. Tozzini Molecular dynamics simulations of enhanced green fluorescent proteins: effects of F64L, S65T and T203Y mutations on the ground-state proton equilibria Proteins: Struct. Funct. Genet. 51 2003 378 389 (Pubitemid 36528823)
    • (2003) Proteins: Structure, Function and Genetics , vol.51 , Issue.3 , pp. 378-389
    • Nifosi, R.1    Tozzini, V.2
  • 9
    • 0035943399 scopus 로고    scopus 로고
    • Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III
    • DOI 10.1016/S0092-8674(01)00462-7
    • D. Jeruzalmi, O. Yurieva, Y. Zhao, M. Young, J. Stewart, M. Hingorani, M. O'Donnell, and J. Kuriyan Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III Cell 106 2001 417 428 (Pubitemid 32786986)
    • (2001) Cell , vol.106 , Issue.4 , pp. 417-428
    • Jeruzalmi, D.1    Yurieva, O.2    Zhao, Y.3    Young, M.4    Stewart, J.5    Hingorani, M.6    O'Donnell, M.7    Kuriyan, J.8
  • 11
    • 77953607331 scopus 로고    scopus 로고
    • The mechanical properties of PCNA: Implications for the loading and function of a DNA sliding clamp
    • J.L. Adelman, J.D. Chodera, I.F. Kuo, T.F. Miller, and D. Barsky The mechanical properties of PCNA: implications for the loading and function of a DNA sliding clamp Biophys. J. 98 2010 3062 3069
    • (2010) Biophys. J. , vol.98 , pp. 3062-3069
    • Adelman, J.L.1    Chodera, J.D.2    Kuo, I.F.3    Miller, T.F.4    Barsky, D.5
  • 12
    • 0000885331 scopus 로고
    • Harmonic analysis of large systems. I. Methodology
    • B.R. Brooks, D. Janezic, and M. Karplus Harmonic analysis of large systems. I. Methodology J. Comp. Chem. 16 1995 1522 1542
    • (1995) J. Comp. Chem. , vol.16 , pp. 1522-1542
    • Brooks, B.R.1    Janezic, D.2    Karplus, M.3
  • 15
    • 0043238084 scopus 로고    scopus 로고
    • Dynamical properties of the MscL of Escherichia coli: A normal mode analysis
    • DOI 10.1016/S0022-2836(03)00851-9
    • H. Valadie, J.J. Lacapere, Y.H. Sanejouand, and C. Etchebest Dynamical properties of the MscL of Escherichia coli: a normal mode analysis J. Mol. Biol. 332 2003 657 674 (Pubitemid 37075988)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.3 , pp. 657-674
    • Valadie, H.1    Lacapcre, J.J.2    Sanejouand, Y.-H.3    Etchebest, C.4
  • 16
    • 28844448877 scopus 로고    scopus 로고
    • Channel opening motion of α7 nicotinic acetylcholine receptor as suggested by normal mode analysis
    • DOI 10.1016/j.jmb.2005.10.039, PII S0022283605012830
    • X. Cheng, B. Lu, B. Grant, R.J. Law, and J.A. McCammon Channel opening motion of alpha7 nicotinic acetylcholine receptor as suggested by normal mode analysis J. Mol. Biol. 355 2006 310 324 (Pubitemid 41774133)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.2 , pp. 310-324
    • Cheng, X.1    Lu, B.2    Grant, B.3    Law, R.J.4    McCammon, J.A.5
  • 17
    • 44449105649 scopus 로고    scopus 로고
    • Effect of cobratoxin binding on the normal mode vibration within acetylcholine binding protein
    • DOI 10.1021/ci700456s
    • E.J. Bertaccini, E. Lindahl, T. Sixma, and J.R. Trudell Effect of cobratoxin binding on the normal mode vibration within acetylcholine binding protein J. Chem. Inf. Model. 48 2008 855 860 (Pubitemid 351757750)
    • (2008) Journal of Chemical Information and Modeling , vol.48 , Issue.4 , pp. 855-860
    • Bertaccini, E.J.1    Lindahl, E.2    Sixma, T.3    Trudell, J.R.4
  • 18
    • 33746794687 scopus 로고    scopus 로고
    • The Open State Gating Mechanism of Gramicidin A Requires Relative Opposed Monomer Rotation and Simultaneous Lateral Displacement
    • DOI 10.1016/j.str.2006.06.007, PII S0969212606002905
    • G. Miloshevsky, and P. Jordan The open state gating mechanism of Gramicidin A requires relative opposed monomer rotation and simultaneous lateral displacement Structure 14 2006 1241 1249 (Pubitemid 44176369)
    • (2006) Structure , vol.14 , Issue.8 , pp. 1241-1249
    • Miloshevsky, G.V.1    Jordan, P.C.2
  • 19
    • 34548706524 scopus 로고    scopus 로고
    • Dynamics of heteropentameric nicotinic acetylcholine receptor: Implications of the gating mechanism
    • DOI 10.1002/prot.21462
    • A. Szarecka, Y. Xu, and P. Tang Dynamics of heteropentameric nicotinic acetylcholine receptor: implications of the gating mechanism Proteins 68 2007 948 960 (Pubitemid 47434716)
    • (2007) Proteins: Structure, Function and Genetics , vol.68 , Issue.4 , pp. 948-960
    • Szarecka, A.1    Xu, Y.2    Tang, P.3
  • 20
    • 22244438519 scopus 로고    scopus 로고
    • Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism
    • DOI 10.1529/biophysj.104.050229
    • A. Taly, M. Delarue, T. Grutter, M. Nilges, N. Le Novere, P.J. Corringer, and J.P. Changeux Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism Biophys. J. 88 2005 3954 3965 (Pubitemid 40991108)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 3954-3965
    • Taly, A.1    Delarue, M.2    Grutter, T.3    Nilges, M.4    Le Novere, N.5    Corringer, P.-J.6    Changeux, J.-P.7
  • 21
    • 0020771265 scopus 로고
    • Dynamics of a small globular proteins in terms of low frequency vibrational modes
    • N. Go, T. Noguti, and T. Nishikawa Dynamics of a small globular proteins in terms of low frequency vibrational modes Proc. Natl. Acad. Sci. U.S.A. 80 1983 3696 3700
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 3696-3700
    • Go, N.1    Noguti, T.2    Nishikawa, T.3
  • 22
    • 80053330768 scopus 로고    scopus 로고
    • Normal mode analysis of trp RNA-binding attenuation protein: Structure and collective motions
    • G. Hu, S. Michielssens, S.L.C. Moors, and A. Ceulemans Normal mode analysis of trp RNA-binding attenuation protein: structure and collective motions J. Chem. Inf. Model. 51 2011 2361 2371
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 2361-2371
    • Hu, G.1    Michielssens, S.2    Moors, S.L.C.3    Ceulemans, A.4
  • 24
    • 77949634796 scopus 로고    scopus 로고
    • Normal mode analysis of biomolecular structures: Functional mechanisms of membrane proteins
    • I. Bahar, T.R. Lezon, A. Bakan, and I.H. Shrivastava Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins Chem. Rev. 110 2009 1463 1497
    • (2009) Chem. Rev. , vol.110 , pp. 1463-1497
    • Bahar, I.1    Lezon, T.R.2    Bakan, A.3    Shrivastava, I.H.4
  • 25
    • 21244444658 scopus 로고    scopus 로고
    • Vibrations-determined properties of green fluorescent protein
    • DOI 10.1002/bip.20264
    • V. Krasnenko, A.H. Tkaczyk, E.R. Tkaczyk, Ö. Farkas, and K. Mauring Vibrations-determined properties of green fluorescent protein Biopolymers 78 2005 140 146 (Pubitemid 40896199)
    • (2005) Biopolymers , vol.78 , Issue.3 , pp. 140-146
    • Krasnenko, V.1    Tkaczyk, A.H.2    Tkaczyk, E.R.3    Farkas, O.4    Mauring, K.5
  • 26
    • 84934444735 scopus 로고    scopus 로고
    • Normal modes and essential dynamics
    • S. Hayward, and B.L. de Groot Normal modes and essential dynamics Methods Mol. Biol. 443 2008 89 106
    • (2008) Methods Mol. Biol. , vol.443 , pp. 89-106
    • Hayward, S.1    De Groot, B.L.2
  • 27
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis
    • M.M. Tirion Large amplitude elastic motions in proteins from a single-parameter atomic analysis Phys. Rev. Lett. 77 1996 1905 1908 (Pubitemid 126625816)
    • (1996) Physical Review Letters , vol.77 , Issue.9 , pp. 1905-1908
    • Tirion, M.M.1
  • 28
    • 0032533790 scopus 로고    scopus 로고
    • Analysis of domain motions by approximate normal mode calculations
    • DOI 10.1002/(SICI)1097-0134(19981 115)33:3<417::AI D-PROT10>3.0.CO;2-8
    • K. Hinsen Analysis of domain motions by approximate normal mode calculations Proteins 33 1998 417 429 (Pubitemid 28516346)
    • (1998) Proteins: Structure, Function and Genetics , vol.33 , Issue.3 , pp. 417-429
    • Hinsen, K.1
  • 29
    • 84857629295 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • I. Bahar, A.R. Atilgan, and B. Erman Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential Fold. Des. 1 1997 357 370
    • (1997) Fold. Des. , vol.1 , pp. 357-370
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 31
  • 32
    • 77953050209 scopus 로고    scopus 로고
    • Perspectives on: Molecular dynamics and computational methods: On the functional significance of soft modes predicted by coarse-grained models for membrane proteins
    • I. Bahar Perspectives on: molecular dynamics and computational methods: on the functional significance of soft modes predicted by coarse-grained models for membrane proteins J. Gen. Physiol. 135 2010 563 573
    • (2010) J. Gen. Physiol. , vol.135 , pp. 563-573
    • Bahar, I.1
  • 33
    • 77952938726 scopus 로고    scopus 로고
    • Global dynamics of proteins: Bridging between structure and function
    • I. Bahar, T.R. Lezon, L.W. Yang, and E. Eyal Global dynamics of proteins: bridging between structure and function Annu. Rev. Biophys. 39 2010 23 42
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 23-42
    • Bahar, I.1    Lezon, T.R.2    Yang, L.W.3    Eyal, E.4
  • 34
    • 17844364634 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: Structure and collective motions
    • DOI 10.1529/biophysj.104.052878
    • A. Hung, K. Tai, and M.S.P. Sansom Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: structure and collective motions Biophys. J. 88 2005 3321 3333 (Pubitemid 40586583)
    • (2005) Biophysical Journal , vol.88 , Issue.5 , pp. 3321-3333
    • Hung, A.1    Tai, K.2    Sansom, M.S.P.3
  • 35
    • 77953553259 scopus 로고    scopus 로고
    • Anharmonic normal mode analysis of elastic network model improves the modeling of atomic fluctuations in protein crystal structures
    • W. Zheng Anharmonic normal mode analysis of elastic network model improves the modeling of atomic fluctuations in protein crystal structures Biophys. J. 98 2010 3025 3034
    • (2010) Biophys. J. , vol.98 , pp. 3025-3034
    • Zheng, W.1
  • 36
    • 77957241496 scopus 로고    scopus 로고
    • Molecular dynamics simulations and elastic network analysis of protein kinase B (Akt/PKB) inactivation
    • S. Cheng, and M.Y. Niv Molecular dynamics simulations and elastic network analysis of protein kinase B (Akt/PKB) inactivation J. Chem. Inf. Model. 50 2010 1602 1610
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 1602-1610
    • Cheng, S.1    Niv, M.Y.2
  • 37
    • 79956095443 scopus 로고    scopus 로고
    • ATP binding enables broad antibiotic selectivity of aminoglycoside phosphotransferase(3)-IIIa: An elastic network analysis
    • S.A. Wieninger, E.H. Serpersu, and G.M. Ullmann ATP binding enables broad antibiotic selectivity of aminoglycoside phosphotransferase(3)-IIIa: an elastic network analysis J. Mol. Biol. 409 2011 450 465
    • (2011) J. Mol. Biol. , vol.409 , pp. 450-465
    • Wieninger, S.A.1    Serpersu, E.H.2    Ullmann, G.M.3
  • 38
    • 78649784550 scopus 로고    scopus 로고
    • Principal component and normal mode analysis of proteins; A quantitative comparison using the GroEL subunit
    • L. Skjaerven, A. Martinez, and N. Reuter Principal component and normal mode analysis of proteins; a quantitative comparison using the GroEL subunit Proteins: Struct. Funct. Bioinf. 79 2011 232 243
    • (2011) Proteins: Struct. Funct. Bioinf. , vol.79 , pp. 232-243
    • Skjaerven, L.1    Martinez, A.2    Reuter, N.3
  • 39
    • 77954614766 scopus 로고    scopus 로고
    • On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm
    • E. Marcos, R. Crehuet, and I. Bahar On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm PLoS Comput. Biol. 6 2010 e1000738
    • (2010) PLoS Comput. Biol. , vol.6 , pp. 1000738
    • Marcos, E.1    Crehuet, R.2    Bahar, I.3
  • 40
    • 25844525600 scopus 로고    scopus 로고
    • The role of shape in determining molecular motions
    • DOI 10.1529/biophysj.105.065904
    • M. Lu, and J. Ma The role of shape in determining molecular motions Biophys. J. 89 2005 2395 2401 (Pubitemid 41401029)
    • (2005) Biophysical Journal , vol.89 , Issue.4 , pp. 2395-2401
    • Lu, M.1    Ma, J.2
  • 41
    • 33745024278 scopus 로고    scopus 로고
    • Symmetry, form, and shape: Guiding principles for robustness in macromolecular machines
    • DOI 10.1146/annurev.biophys.35.040405.102010
    • F. Tama, and C.L. Brooks Symmetry, form, and shape: guiding principles for robustness in macromolecular machines Annu. Rev. Biophys. Biomol. 35 2006 115 133 (Pubitemid 43877372)
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 115-133
    • Tama, F.1    Brooks III, C.L.2
  • 42
    • 0036077875 scopus 로고    scopus 로고
    • Simplified normal mode analysis of conformational transitions in DNA-dependent polymerases: The Elastic Network Model
    • DOI 10.1016/S0022-2836(02)00562-4
    • M. Delarue, and Y.H. Sanejouand Simplified normal mode analysis of conformational transitions in DNA-dependent polymerases: the elastic network model J. Mol. Biol. 320 2002 1011 1024 (Pubitemid 34808821)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.5 , pp. 1011-1024
    • Delarue, M.1    Sanejouand, Y.-H.2
  • 43
    • 0032576730 scopus 로고    scopus 로고
    • Toroidal proteins: Running rings around DNA
    • M.M. Hingorani, and M. O'Donnell Toroidal proteins: running rings around DNA Curr. Biol. 8 1998 R83 R86
    • (1998) Curr. Biol. , vol.8
    • Hingorani, M.M.1    O'Donnell, M.2
  • 44
    • 0028292635 scopus 로고
    • Harmonic and anharmonic aspects in the dynamics of BPTI: A normal mode analysis and principal component analysis
    • S. Hayward, A. Kitao, and N. Go Harmonic and anharmonic aspects in the dynamics of PBTI: a normal mode analysis and principal component analysis Protein Sci. 3 1994 936 943 (Pubitemid 24170073)
    • (1994) Protein Science , vol.3 , Issue.6 , pp. 936-943
    • Hayward, S.1    Kitao, A.2    Go, N.3
  • 45
    • 38949218425 scopus 로고    scopus 로고
    • Close Correspondence between the Motions from Principal Component Analysis of Multiple HIV-1 Protease Structures and Elastic Network Modes
    • DOI 10.1016/j.str.2007.12.011, PII S0969212608000117
    • L. Yang, G. Song, A. Carriquiry, and R.L. Jernigan Close correspondence between the motions from principal component analysis of multiple HIV-1 protease structures and elastic network modes Structure 16 2008 321 330 (Pubitemid 351215213)
    • (2008) Structure , vol.16 , Issue.2 , pp. 321-330
    • Yang, L.1    Song, G.2    Carriquiry, A.3    Jernigan, R.L.4
  • 46
    • 33846189408 scopus 로고    scopus 로고
    • Interpreting Correlated Motions Using Normal Mode Analysis
    • DOI 10.1016/j.str.2006.09.003, PII S0969212606003893
    • A.W. van Wynsberghe, and Q. Cui Interpreting correlated motions using normal mode analysis Structure 14 2006 1647 1653 (Pubitemid 46107270)
    • (2006) Structure , vol.14 , Issue.11 , pp. 1647-1653
    • Van Wynsberghe, A.W.1    Cui, Q.2
  • 47
    • 5444228752 scopus 로고    scopus 로고
    • Normal-mode analysis suggests protein flexibility modulation throughout RNA polymerase's functional cycle
    • DOI 10.1021/bi049738+
    • A. van Wynsberghe, G.H. Li, and Q. Cui Normal-mode analysis suggests protein flexibility modulation throughout RNA polymerase's functional cycle Biochemistry 43 2004 13083 13096 (Pubitemid 39362778)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 13083-13096
    • Van Wynsberghe, A.1    Li, G.2    Cui, Q.3
  • 48
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and 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    Van Der Spoel, D.3    Lindahl, E.4
  • 50
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat
    • T.E. Cheatham 3rd, P. Cieplak, and P.A. Kollman A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat J. Biomol. Struct. Dyn. 16 1999 845 862 (Pubitemid 29157655)
    • (1999) Journal of Biomolecular Structure and Dynamics , vol.16 , Issue.4 , pp. 845-862
    • Cheatham III, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 51
    • 33747858757 scopus 로고    scopus 로고
    • NOMAD-Ref: Visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis
    • E. Lindahl, C. Azuara, P. Koehl, and M. Delarue NOMAD-Ref: visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis Nucleic Acids Res. 34 2006 52 56
    • (2006) Nucleic Acids Res. , vol.34 , pp. 52-56
    • Lindahl, E.1    Azuara, C.2    Koehl, P.3    Delarue, M.4
  • 54
    • 0006548250 scopus 로고
    • The vibrations of annular and globular molecules - Theory
    • A. Ceulemans, and I. Vos The vibrations of annular and globular molecules - theory Mol. Phys. 72 1991 1051 1080
    • (1991) Mol. Phys. , vol.72 , pp. 1051-1080
    • Ceulemans, A.1    Vos, I.2
  • 55
    • 41149141017 scopus 로고    scopus 로고
    • Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis
    • DOI 10.1002/prot.21787
    • M.Y. Niv, and M. Filizola Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis Proteins: Struct. Funct. Bioinf. 71 2008 575 586 (Pubitemid 351429999)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.2 , pp. 575-586
    • Niv, M.Y.1    Filizola, M.2
  • 56
    • 84860389205 scopus 로고    scopus 로고
    • Predicting large-scale conformational changes in proteins using energy-weighted normal modes
    • D.S. Palmer, and F. Jensen Predicting large-scale conformational changes in proteins using energy-weighted normal modes Proteins 79 2011 2778 2793
    • (2011) Proteins , vol.79 , pp. 2778-2793
    • Palmer, D.S.1    Jensen, F.2
  • 58
    • 0022106012 scopus 로고
    • Low-frequency motions in protein molecules: Beta-sheet and beta-barrel
    • K.C. Chou Low-frequency motions in protein molecules: beta-sheet and beta-barrel Biophys. J. 48 1985 289 297
    • (1985) Biophys. J. , vol.48 , pp. 289-297
    • Chou, K.C.1
  • 60
    • 0036283344 scopus 로고    scopus 로고
    • Sequence-dependent motions of DNA: A normal mode analysis at the base-pair level
    • A. Matsumoto, and W.K. Olson Sequence-dependent motions of DNA: a normal mode analysis at the base-pair level Biophys. J. 83 2002 22 41 (Pubitemid 34694718)
    • (2002) Biophysical Journal , vol.83 , Issue.1 , pp. 22-41
    • Matsumoto, A.1    Olson, W.K.2
  • 61
    • 43849085010 scopus 로고    scopus 로고
    • The elastic properties of the structurally characterized myosin II S2 subdomain: A molecular dynamics and normal mode analysis
    • I. Adamovich, S.M. Mijailovich, and M. Karplus The elastic properties of the structurally characterized myosin II S2 subdomain: a molecular dynamics and normal mode analysis Biophys. J. 94 2008 3779 3789
    • (2008) Biophys. J. , vol.94 , pp. 3779-3789
    • Adamovich, I.1    Mijailovich, S.M.2    Karplus, M.3
  • 63
    • 79959799630 scopus 로고    scopus 로고
    • Escherichia coli processivity clamp β from polymerase III is dynamic in solution
    • J. Fang, J.R. Engen, and P.J. Beuning Escherichia coli processivity clamp β from polymerase III is dynamic in solution Biochemistry 50 2011 5958 5968
    • (2011) Biochemistry , vol.50 , pp. 5958-5968
    • Fang, J.1    Engen, J.R.2    Beuning, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.