메뉴 건너뛰기




Volumn 25, Issue 2, 2011, Pages 181-194

Structural-dynamical investigation of the ZnuA histidine-rich loop: Involvement in zinc management and transport

Author keywords

ABC transporter family; Histidine rich loop; Molecular dynamics simulation; Zinc transport; ZnuA

Indexed keywords

AMINO ACIDS; ESCHERICHIA COLI; PROTEINS; SALMONELLA; X RAY DIFFRACTION; ZINC;

EID: 79951676150     PISSN: 0920654X     EISSN: 15734951     Source Type: Journal    
DOI: 10.1007/s10822-010-9409-6     Document Type: Article
Times cited : (16)

References (50)
  • 1
    • 55949093712 scopus 로고    scopus 로고
    • Metal ions in biological catalysis: From enzyme databases to general principles
    • 1:CAS:528:DC%2BD1cXhtlGgtr%2FP 10.1007/s00775-008-0404-5
    • C Andreini I Bertini G Cavallaro GL Holliday JM Thornton 2008 Metal ions in biological catalysis: from enzyme databases to general principles J Biol Inorg Chem 13 1205 1218 1:CAS:528:DC%2BD1cXhtlGgtr%2FP 10.1007/s00775-008-0404-5
    • (2008) J Biol Inorg Chem , vol.13 , pp. 1205-1218
    • Andreini, C.1    Bertini, I.2    Cavallaro, G.3    Holliday, G.L.4    Thornton, J.M.5
  • 2
    • 36749092727 scopus 로고    scopus 로고
    • 2+ uptake system ZnuABC is required for bacterial zinc homeostasis in intracellular environments and contributes to the virulence of Salmonella enterica
    • DOI 10.1128/IAI.00559-07
    • 2+ uptake system ZnuABC is required for bacterial zinc homeostasis in intracellular environments and contributes to the virulence of Salmonella enterica Infect Immun 75 5867 5876 1:CAS:528:DC%2BD2sXhsVWit7jL 10.1128/IAI.00559-07 (Pubitemid 350207826)
    • (2007) Infection and Immunity , vol.75 , Issue.12 , pp. 5867-5876
    • Ammendola, S.1    Pasquali, P.2    Pistoia, C.3    Petrucci, P.4    Petrarca, P.5    Rotilio, G.6    Battistoni, A.7
  • 3
    • 15744394198 scopus 로고    scopus 로고
    • Bacterial zinc uptake and regulators
    • DOI 10.1016/j.mib.2005.02.001, Cell Regulation
    • K Hantke 2005 Bacterial zinc uptake and regulators Curr Opin Microbiol 8 196 202 1:CAS:528:DC%2BD2MXivFSltrs%3D 10.1016/j.mib.2005.02.001 (Pubitemid 40417962)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.2 , pp. 196-202
    • Hantke, K.1
  • 4
    • 61449341855 scopus 로고    scopus 로고
    • Structure and mechanism of ATP-binding cassette transporters
    • 1:CAS:528:DC%2BD1MXivFSltLs%3D 10.1098/rstb.2008.0125
    • KP Locher 2009 Structure and mechanism of ATP-binding cassette transporters Phil Trans R Soc B 364 239 245 1:CAS:528:DC%2BD1MXivFSltLs%3D 10.1098/rstb.2008.0125
    • (2009) Phil Trans R Soc B , vol.364 , pp. 239-245
    • Locher, K.P.1
  • 5
    • 60749083913 scopus 로고    scopus 로고
    • ABC transporters: The power to change
    • 1:CAS:528:DC%2BD1MXitFKlsL0%3D 10.1038/nrm2646
    • DC Rees E Johnson O Lewinson 2009 ABC transporters: the power to change Nat Rev Mol Cell Biol 10 218 227 1:CAS:528:DC%2BD1MXitFKlsL0%3D 10.1038/nrm2646
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 218-227
    • Rees, D.C.1    Johnson, E.2    Lewinson, O.3
  • 6
    • 34247269203 scopus 로고    scopus 로고
    • Crystal Structure of the Zinc-binding Transport Protein ZnuA from Escherichia coli Reveals an Unexpected Variation in Metal Coordination
    • DOI 10.1016/j.jmb.2007.02.107, PII S0022283607002963
    • H Li G Jogl 2007 Crystal structure of the zinc-binding transport protein ZnuA from Escherichia coli reveals an unexpected variation in metal coordination J Mol Biol 368 1358 1366 1:CAS:528:DC%2BD2sXkslCms7Y%3D 10.1016/j.jmb.2007.02. 107 (Pubitemid 46617595)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.5 , pp. 1358-1366
    • Li, H.1    Jogl, G.2
  • 7
    • 33847702525 scopus 로고    scopus 로고
    • Structural Analysis of ABC-family Periplasmic Zinc Binding Protein Provides New Insights Into Mechanism of Ligand Uptake and Release
    • DOI 10.1016/j.jmb.2007.01.041, PII S0022283607000812
    • BR Chandra M Yogavel A Sharma 2007 Structural analysis of ABC-family periplasmic zinc binding protein provides new insights into mechanism of ligand uptake and release J Mol Biol 367 970 982 1:CAS:528:DC%2BD2sXjtFKit70%3D 10.1016/j.jmb.2007.01.041 (Pubitemid 46386071)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.4 , pp. 970-982
    • Chandra, B.R.1    Yogavel, M.2    Sharma, A.3
  • 9
    • 34547646347 scopus 로고    scopus 로고
    • Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA
    • DOI 10.1021/bi700763w
    • B Wei AM Randich M Bhattacharyya-Pakrasi HB Pakrasi TJ Smith 2007 Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA Biochemistry 46 8734 8743 1:CAS:528:DC%2BD2sXns1Cksrs%3D 10.1021/bi700763w (Pubitemid 47204439)
    • (2007) Biochemistry , vol.46 , Issue.30 , pp. 8734-8743
    • Wei, B.1    Randich, A.M.2    Bhattacharyya-Pakrasi, M.3    Pakrasi, H.B.4    Smith, T.J.5
  • 10
    • 0142216623 scopus 로고    scopus 로고
    • Structural determinants of metal specificity in the zinc transport protein ZnuA from Synechocystis 6803
    • DOI 10.1016/j.jmb.2003.09.008
    • S Banerjee B Wei M Bhattacharyya-Pakrasi HB Pakrasi Smith Tj 2003 Structural determinants of metal specificity in the zinc transport protein ZnuA from Synechocystis 6803 J Mol Biol 333 1061 1069 1:CAS:528:DC%2BD3sXosVynsr8%3D 10.1016/j.jmb.2003.09.008 (Pubitemid 37324505)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.5 , pp. 1061-1069
    • Banerjee, S.1    Wei, B.2    Bhattacharyya-Pakrasi, M.3    Pakrasi, H.B.4    Smith, T.J.5
  • 11
    • 0035011106 scopus 로고    scopus 로고
    • A new family of high-affinity ABC manganese and zinc permeases
    • DOI 10.1016/S0923-2508(01)01195-0
    • JP Claverys 2001 A new family of high-affinity ABC manganese and zinc permeases Res Microbiol 152 231 243 1:CAS:528:DC%2BD3MXks12js78%3D 10.1016/S0923-2508(01)01195-0 (Pubitemid 32436482)
    • (2001) Research in Microbiology , vol.152 , Issue.3-4 , pp. 231-243
    • Claverys, J.-P.1
  • 12
    • 3042633867 scopus 로고    scopus 로고
    • Periplasmic competition for zinc uptake between the metallochaperone ZnuA and Cu,Zn superoxide dismutase
    • DOI 10.1016/j.febslet.2004.06.008, PII S0014579304007252
    • G Berducci AP Mazzetti G Rotilio A Battistoni 2004 Periplasmic competition for zinc uptake between the metallochaperone ZnuA and Cu, Zn superoxide dismutase FEBS Lett 569 289 292 1:CAS:528:DC%2BD2cXlt1amu7w%3D 10.1016/j.febslet.2004.06.008 (Pubitemid 38844634)
    • (2004) FEBS Letters , vol.569 , Issue.1-3 , pp. 289-292
    • Berducci, G.1    Mazzetti, A.P.2    Rotilio, G.3    Battistoni, A.4
  • 13
    • 34250634316 scopus 로고    scopus 로고
    • 2+ (Znu) transporters in Treponema pallidum: Analysis of metal specificities and expression profiles
    • DOI 10.1111/j.1365-2958.2007.05771.x
    • DC Desrosiers YC Sun AA Zaidi CH Eggers DL Cox JD Radolf 2007 The general transition metal (Tro) and Zn2(Znu) transporters in Treponema pallidum: analysis of metal specificities and expression profiles Mol Microbiol 65 137 152 1:CAS:528:DC%2BD2sXnslyjt70%3D 10.1111/j.1365-2958.2007.05771.x (Pubitemid 46934485)
    • (2007) Molecular Microbiology , vol.65 , Issue.1 , pp. 137-152
    • Desrosiers, D.C.1    Sun, Y.C.2    Zaidi, A.A.3    Eggers, C.H.4    Cox, D.L.5    Radolf, J.D.6
  • 14
    • 77949409266 scopus 로고    scopus 로고
    • The Zur-regulated ZinT protein is an auxiliary component of the high-affinity ZnuABC zinc transporter that facilitates metal recruitment during severe zinc shortage
    • 1:CAS:528:DC%2BC3cXjsl2gtL0%3D 10.1128/JB.01310-09
    • P Petrarca S Ammendola P Pasquali A Battistoni 2010 The Zur-regulated ZinT protein is an auxiliary component of the high-affinity ZnuABC zinc transporter that facilitates metal recruitment during severe zinc shortage J Bacteriol 192 1553 1564 1:CAS:528:DC%2BC3cXjsl2gtL0%3D 10.1128/JB.01310-09
    • (2010) J Bacteriol , vol.192 , pp. 1553-1564
    • Petrarca, P.1    Ammendola, S.2    Pasquali, P.3    Battistoni, A.4
  • 15
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • K Arnold L Bordoli J Kopp T Schwede 2006 The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22 195 201 1:CAS:528:DC%2BD28XovVCltw%3D%3D 10.1093/bioinformatics/bti770 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 16
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • DOI 10.1002/prot.1168
    • PA Bates LA Kelley RM MacCallum MJE Sternberg 2001 Enhancement of protein modelling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM Proteins Struct Funct Gen 5 39 46 10.1002/prot.1168 (Pubitemid 34113166)
    • (2001) Proteins: Structure, Function and Genetics , vol.45 , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.E.4
  • 17
    • 79951681330 scopus 로고    scopus 로고
    • CpHModels-30 remote homology modeling using structure guided profile sequence alignment and double-sided baseline corrected scoring scheme
    • 3-7 Dec, Cagliari, Sardinia, Italy
    • Nielsen M, Lundegaard C, Lund O, Petersen TN (2008) CpHModels-30 remote homology modeling using structure guided profile sequence alignment and double-sided baseline corrected scoring scheme. CASP8 conference, 3-7 Dec, Cagliari, Sardinia, Italy, p 193
    • (2008) CASP8 Conference , pp. 193
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Petersen, T.N.4
  • 18
    • 77949434706 scopus 로고    scopus 로고
    • Modeling of loops in proteins: A multi-method approach
    • 10.1186/1472-6807-10-5
    • M Jamroz A Kolinski 2010 Modeling of loops in proteins: a multi-method approach BMC Struct Biol 10 5 10.1186/1472-6807-10-5
    • (2010) BMC Struct Biol , vol.10 , pp. 5
    • Jamroz, M.1    Kolinski, A.2
  • 20
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 1:CAS:528:DyaK3sXit12lurY%3D 10.1107/S0021889892009944
    • RA Laskowski MW MacArthur DS Moss JM Thornton 1993 PROCHECK: a program to check the stereochemical quality of protein structures J Appl Cryst 26 283 291 1:CAS:528:DyaK3sXit12lurY%3D 10.1107/S0021889892009944
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 21
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • 10.1093/nar/gkm216
    • IW Davis L Weston Murray JS Richardson DC Richardson 2007 MolProbity: all-atom contacts and structure validation for proteins and nucleic acids Nucleic Acids Res 35 375 383 10.1093/nar/gkm216
    • (2007) Nucleic Acids Res , vol.35 , pp. 375-383
    • Davis, I.W.1    Weston Murray, L.2    Richardson, J.S.3    Richardson, D.C.4
  • 25
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • 1:CAS:528:DC%2BD3sXovVygsbc%3D 10.1002/jcc.10349
    • Y Duan C Wu S Chowdhury MC Lee G Xiong W Zhang R Yang P Cieplak R Luo T Lee J Caldwell J Wang P Kollman 2003 A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations J Comput Chem 24 1999 2012 1:CAS:528:DC%2BD3sXovVygsbc%3D 10.1002/jcc.10349
    • (2003) J Comput Chem , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6    Yang, R.7    Cieplak, P.8    Luo, R.9    Lee, T.10    Caldwell, J.11    Wang, J.12    Kollman, P.13
  • 26
    • 0036606163 scopus 로고    scopus 로고
    • Flexibility in monomeric Cu,Zn superoxide dismutase detected by limited proteolysis and molecular dynamics simulation
    • DOI 10.1002/prot.10094
    • M Falconi L Parrilli A Battistoni A Desideri 2002 Protein flexibility in monomeric Cu, Zn superoxide dismutase detected by molecular dynamics simulation and limited proteolysis Proteins Struct Funct Genet 47 513 520 1:CAS:528:DC%2BD38XksVyqu7Y%3D 10.1002/prot.10094 (Pubitemid 34614731)
    • (2002) Proteins: Structure, Function and Genetics , vol.47 , Issue.4 , pp. 513-520
    • Falconi, M.1    Parrilli, L.2    Battistoni, A.3    Desideri, A.4
  • 27
    • 0029115487 scopus 로고
    • Zinc binding in proteins and solution: A simple but accurate nonbonded representation
    • 1:CAS:528:DyaK2MXosVWrtLg%3D 10.1002/prot.340230104
    • R Stote M Karplus 1995 Zinc binding in proteins and solution: a simple but accurate nonbonded representation Proteins Struct Funct Genet 23 12 31 1:CAS:528:DyaK2MXosVWrtLg%3D 10.1002/prot.340230104
    • (1995) Proteins Struct Funct Genet , vol.23 , pp. 12-31
    • Stote, R.1    Karplus, M.2
  • 29
    • 16844373030 scopus 로고    scopus 로고
    • Zn protein simulations including charge transfer and local polarization effects
    • DOI 10.1021/ja0429115
    • DV Sakharov C Lim 2005 Zn protein simulations including charge transfer and local polarization effects J Am Chem Soc 127 4921 4929 1:CAS:528: DC%2BD2MXit1Ojurs%3D 10.1021/ja0429115 (Pubitemid 40489646)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.13 , pp. 4921-4929
    • Sakharov, D.V.1    Lim, C.2
  • 30
    • 58249086106 scopus 로고    scopus 로고
    • Force fields including charge transfer and local polarization effects: Application to proteins containing multi/heavy metal ions
    • 1:CAS:528:DC%2BD1MXns1Wgtw%3D%3D 10.1002/jcc.21048
    • DV Sakharov C Lim 2009 Force fields including charge transfer and local polarization effects: application to proteins containing multi/heavy metal ions J Comput Chem 30 191 202 1:CAS:528:DC%2BD1MXns1Wgtw%3D%3D 10.1002/jcc.21048
    • (2009) J Comput Chem , vol.30 , pp. 191-202
    • Sakharov, D.V.1    Lim, C.2
  • 32
    • 0000510540 scopus 로고    scopus 로고
    • Novel zinc protein molecular dynamics simulations: Steps toward antiangiogenesis for cancer treatment
    • 1:CAS:528:DyaK1MXmvVSktbw%3D 10.1007/s008940050119
    • YP Pang 1999 Novel zinc protein molecular dynamics simulations: steps toward antiangiogenesis for cancer treatment J Mol Model 5 196 202 1:CAS:528:DyaK1MXmvVSktbw%3D 10.1007/s008940050119
    • (1999) J Mol Model , vol.5 , pp. 196-202
    • Pang, Y.P.1
  • 33
    • 0033769641 scopus 로고    scopus 로고
    • Successful molecular dynamics simulation of the zinc-bound farnesyltransferase using the cationic dummy atom approach
    • 1:CAS:528:DC%2BD3cXosFKksLo%3D
    • YP Pang K Xu J El Yazal FG Prendergast 2000 Successful molecular dynamics simulation of the zinc-bound farnesyltransferase using the cationic dummy atom approach Protein Sci 9 1857 1865 1:CAS:528:DC%2BD3cXosFKksLo%3D
    • (2000) Protein Sci , vol.9 , pp. 1857-1865
    • Pang, Y.P.1    Xu, K.2    El Yazal, J.3    Prendergast, F.G.4
  • 34
    • 0035889687 scopus 로고    scopus 로고
    • Successful molecular dynamics simulation of two zinc complexes bridged by a hydroxide in phosphotriesterase using the cationic dummy atom method
    • DOI 10.1002/prot.1138
    • YP Pang 2001 Successful molecular dynamics simulation of two zinc complexes bridged by a hydroxide in phosphotriesterase using the cationic dummy atom method Proteins 45 183 189 1:CAS:528:DC%2BD3MXot12rsbo%3D 10.1002/prot.1138 (Pubitemid 32988580)
    • (2001) Proteins: Structure, Function and Genetics , vol.45 , Issue.3 , pp. 183-189
    • Pang, Y.-P.1
  • 35
    • 0000020246 scopus 로고    scopus 로고
    • A five-site model for liquid water and the reproduction of the density anomaly by rigid, nonpolarizable potential functions
    • 10.1063/1.481505
    • WL Jorgensen MW Mahoney 2000 A five-site model for liquid water and the reproduction of the density anomaly by rigid, nonpolarizable potential functions J Chem Phys 112 8910 8922 10.1063/1.481505
    • (2000) J Chem Phys , vol.112 , pp. 8910-8922
    • Jorgensen, W.L.1    Mahoney, M.W.2
  • 36
    • 33846823909 scopus 로고
    • Particle mesh Ewald an N-log(n) method for Ewald sums in large systems
    • 1:CAS:528:DyaK3sXks1Ohsr0%3D 10.1063/1.464397
    • T Darden D York L Pedersen 1993 Particle mesh Ewald an N-log(n) method for Ewald sums in large systems J Chem Phys 98 10089 10092 1:CAS:528: DyaK3sXks1Ohsr0%3D 10.1063/1.464397
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 37
    • 0029170114 scopus 로고
    • Molecular dynamics simulation on solvated biomolecular systems: The particle mesh Ewald method leads to stable trajectories of DNA, RNA and proteins
    • 1:CAS:528:DyaK2MXkvVaisrc%3D 10.1021/ja00119a045
    • TE Cheatham JL Miller T Fox TA Darden PA Kollman 1995 Molecular dynamics simulation on solvated biomolecular systems: the particle mesh Ewald method leads to stable trajectories of DNA, RNA and proteins J Am Chem Soc 117 4193 4194 1:CAS:528:DyaK2MXkvVaisrc%3D 10.1021/ja00119a045
    • (1995) J Am Chem Soc , vol.117 , pp. 4193-4194
    • Cheatham, T.E.1    Miller, J.L.2    Fox, T.3    Darden, T.A.4    Kollman, P.A.5
  • 38
    • 0034506266 scopus 로고    scopus 로고
    • Efficient particle-mesh Ewald based approach to fixed and induced dipolar interactions
    • DOI 10.1063/1.1324708
    • A Toukmaji C Sagui J Board T Darden 2000 Efficient particle-mesh Ewald based approach to fixed and induced dipolar interactions J Chem Phys 113 10913 10927 1:CAS:528:DC%2BD3cXovVKhsb0%3D 10.1063/1.1324708 (Pubitemid 32087579)
    • (2000) Journal of Chemical Physics , vol.113 , Issue.24 , pp. 10913-10927
    • Toukmaji, A.1    Sagui, C.2    Board, J.3    Darden, T.4
  • 39
    • 48749137581 scopus 로고
    • Stochastic boundary conditions for molecular dynamics simulations of ST2 water
    • 10.1016/0009-2614(84)80098-6
    • A Brünger CL Brooks III M Karplus 1984 Stochastic boundary conditions for molecular dynamics simulations of ST2 water Chem Phys Lett 105 495 500 10.1016/0009-2614(84)80098-6
    • (1984) Chem Phys Lett , vol.105 , pp. 495-500
    • Brünger, A.1    Brooks Iii, C.L.2    Karplus, M.3
  • 40
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • 1:CAS:528:DyaK2cXmtFeht7o%3D 10.1063/1.467468
    • GJ Martyna DJ Tobias ML Klein 1994 Constant pressure molecular dynamics algorithms J Chem Phys 101 4177 4189 1:CAS:528:DyaK2cXmtFeht7o%3D 10.1063/1.467468
    • (1994) J Chem Phys , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 41
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • 1:CAS:528:DyaK2MXotVentLo%3D 10.1063/1.470648
    • SE Feller Y Zhang RW Pastor BR Brooks 1995 Constant pressure molecular dynamics simulation: the Langevin piston method J Chem Phys 103 4613 4621 1:CAS:528:DyaK2MXotVentLo%3D 10.1063/1.470648
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 42
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • 1:CAS:528:DyaE2sXktVGhsL4%3D 10.1016/0021-9991(77)90098-5
    • JP Ryckaert G Ciccotti HJC Berendsen 1977 Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J Comput Phys 23 327 341 1:CAS:528:DyaE2sXktVGhsL4%3D 10.1016/0021-9991(77)90098-5
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 43
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • 1:CAS:528:DyaK38Xlslykt7o%3D 10.1002/jcc.540130805
    • S Miyamoto PA Kollman 1992 Settle: an analytical version of the SHAKE and RATTLE algorithm for rigid water models J Comp Chem 13 952 962 1:CAS:528:DyaK38Xlslykt7o%3D 10.1002/jcc.540130805
    • (1992) J Comp Chem , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 44
    • 0000577041 scopus 로고
    • Large-amplitude nonlinear motions in proteins
    • 1:CAS:528:DyaK38XkvVGntLc%3D 10.1103/PhysRevLett.68.2696
    • AE Garcia 1992 Large-amplitude nonlinear motions in proteins Phys Rev Lett 68 2696 2699 1:CAS:528:DyaK38XkvVGntLc%3D 10.1103/PhysRevLett.68.2696
    • (1992) Phys Rev Lett , vol.68 , pp. 2696-2699
    • Garcia, A.E.1
  • 46
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • 1:CAS:528:DC%2BD1cXhsVSqurc%3D 10.1021/ct700301q
    • B Hess C Kutzner D van der Spoel E Lindahl 2008 GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J Chem Theory Comput 4 435 447 1:CAS:528:DC%2BD1cXhsVSqurc%3D 10.1021/ct700301q
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 47
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • 10.1016/0010-4655(95)00042-E
    • HJC Berendsen D van der Spool R van Drunen 1995 GROMACS: a message-passing parallel molecular dynamics implementation Comput Phys Commun 95 43 56 10.1016/0010-4655(95)00042-E
    • (1995) Comput Phys Commun , vol.95 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spool, D.2    Van Drunen, R.3
  • 48
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College London
    • Hubbard SJ, Thornton JM (1993) NACCESS, computer program. Department of Biochemistry and Molecular Biology, University College, London
    • (1993) NACCESS, Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 49
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • DOI 10.1016/0263-7855(96)00018-5
    • W Humphrey A Dalke K Schulten 1996 VMD: visual molecular dynamics J Mol Graph 14 33 38 1:CAS:528:DyaK28Xis12nsrg%3D 10.1016/0263-7855(96)00018-5 (Pubitemid 26152973)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 50
    • 0026655361 scopus 로고
    • Stereochemical quality of protein structure coordinates
    • 1:CAS:528:DyaK38XisFWls7o%3D 10.1002/prot.340120407
    • AL Morris MW MacArthur EG Hutchinson JM Thornton 1992 Stereochemical quality of protein structure coordinates Proteins Struct Funct Genet 12 345 364 1:CAS:528:DyaK38XisFWls7o%3D 10.1002/prot.340120407
    • (1992) Proteins Struct Funct Genet , vol.12 , pp. 345-364
    • Morris, A.L.1    MacArthur, M.W.2    Hutchinson, E.G.3    Thornton, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.