메뉴 건너뛰기




Volumn 10, Issue 1, 2009, Pages

Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARTIC ACID; CYSTEINE; IRON SULFUR PROTEIN; SCAFFOLD PROTEIN; BACTERIAL PROTEIN;

EID: 60649117402     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-10-3     Document Type: Article
Times cited : (44)

References (46)
  • 1
    • 0036670725 scopus 로고    scopus 로고
    • Biosynthesis of iron-sulphur clusters is a complex and highly conserved process
    • 10.1042/BST0300680. 12196163
    • Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. J Frazzon JR Fick DR Dean, Biochem Soc Trans 2002 30 4 680 685 10.1042/BST0300680 12196163
    • (2002) Biochem Soc Trans , vol.30 , Issue.4 , pp. 680-685
    • Frazzon, J.1    Fick, J.R.2    Dean, D.R.3
  • 2
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry
    • 10.1016/S1367-5931(03)00021-8
    • Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry. J Frazzon DR Dean, Curr Opinion Cheml Biol 2003 7 166 173 10.1016/S1367-5931(03)00021-8
    • (2003) Curr Opinion Cheml Biol , vol.7 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 3
    • 20744446399 scopus 로고    scopus 로고
    • Structure, Function and Formation of Biological Iron-Sulfur Clusters
    • 10.1146/annurev.biochem.74.082803.133518. 15952888
    • Structure, Function and Formation of Biological Iron-Sulfur Clusters. DC Johnson DR Dean AD Smith MK Johnson, Annu Rev Biochem 2005 74 247 81 10.1146/annurev.biochem.74.082803.133518 15952888
    • (2005) Annu Rev Biochem , vol.74 , pp. 247-81
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 4
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases
    • 10.1146/annurev.biochem.76.052705.162653. 18366324
    • Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases. R Lill U Mühlenhoff, Annu Rev Biochem 2008 77 669 700 10.1146/annurev.biochem.76.052705.162653 18366324
    • (2008) Annu Rev Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 5
    • 0014024195 scopus 로고
    • The reconstitution of Clostridial ferredoxin
    • 10.1016/0006-291X(66)90561-4. 5962494
    • The reconstitution of Clostridial ferredoxin. R Malkin JC Rabinowitz, Biochem Biophys Res Comm 1966 23 822 827 10.1016/0006-291X(66)90561-4 5962494
    • (1966) Biochem Biophys Res Comm , vol.23 , pp. 822-827
    • Malkin, R.1    Rabinowitz, J.C.2
  • 6
    • 0003721012 scopus 로고    scopus 로고
    • RP Hausinger GL Eichorn LG Marzilli Eds, New York: Wiley
    • RP Hausinger GL Eichorn LG Marzilli Eds, Mechanisms of Metallocenter Assembly New York: Wiley 1996
    • (1996) Mechanisms of Metallocenter Assembly
  • 7
    • 0033120863 scopus 로고    scopus 로고
    • Fe-S proteins in sensing and regulatory functions
    • 10.1016/S1367-5931(99)80027-1. 10226040
    • Fe-S proteins in sensing and regulatory functions. H Beinert PJ Kiley, Curr Opin Chem Biol 1999 3 2 152 7 10.1016/S1367-5931(99)80027-1 10226040
    • (1999) Curr Opin Chem Biol , vol.3 , Issue.2 , pp. 152-7
    • Beinert, H.1    Kiley, P.J.2
  • 8
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: Ancient structures, still full of surprises
    • 10.1007/s007750050002. 10766431
    • Iron-sulfur proteins: ancient structures, still full of surprises. H Beinert, J Biol Inorg Chem 2000 5 1 2 15 10.1007/s007750050002 10766431
    • (2000) J Biol Inorg Chem , vol.5 , Issue.1 , pp. 2-15
    • Beinert, H.1
  • 9
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • 10.1016/S1369-5274(03)00039-0. 12732309
    • The role of Fe-S proteins in sensing and regulation in bacteria. PJ Kiley H Beinert, Curr Opin Microbiol 2003 6 2 181 5 10.1016/S1369-5274(03)00039-0 12732309
    • (2003) Curr Opin Microbiol , vol.6 , Issue.2 , pp. 181-5
    • Kiley, P.J.1    Beinert, H.2
  • 11
    • 0024743814 scopus 로고
    • Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii
    • 10.1007/BF00261156. 2615765
    • Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii. MR Jacobson VL Cash MC Weiss NF Laird WE Newton DR Dean, Mol Gen Genet 1989 219 49 57 10.1007/BF00261156 2615765
    • (1989) Mol Gen Genet , vol.219 , pp. 49-57
    • Jacobson, M.R.1    Cash, V.L.2    Weiss, M.C.3    Laird, N.F.4    Newton, W.E.5    Dean, D.R.6
  • 12
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron sulfur clusters: Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • 10.1074/jbc.273.21.13264. 9582371
    • Assembly of iron sulfur clusters: identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. L Zheng VL Cash DH Flint DR Dean, J Biol Chem 1998 273 13264 13272 10.1074/jbc.273.21.13264 9582371
    • (1998) J Biol Chem , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 13
    • 27744499033 scopus 로고    scopus 로고
    • Mechanisms of iron-sulfur cluster assembly: The SUF machinery
    • 10.1007/s00775-005-0025-1. 16211402
    • Mechanisms of iron-sulfur cluster assembly: the SUF machinery. M Fontecave S Ollagnier de Choudens F Barras, J Biol Inorg Chem 2005 10 713 721 10.1007/s00775-005-0025-1 16211402
    • (2005) J Biol Inorg Chem , vol.10 , pp. 713-721
    • Fontecave, M.1    Ollagnier De Choudens, S.2    Barras, F.3
  • 14
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archea and plastids
    • 10.1074/jbc.C200365200. 12089140
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archea and plastids. Y Takahashi U Tokumoto, J Biol Chem 2002 277 28380 28383 10.1074/jbc.C200365200 12089140
    • (2002) J Biol Chem , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 15
    • 4644221775 scopus 로고    scopus 로고
    • Iron-Sulfur Cluster Biosynthesis: Toward an Understanding of Cellular Machinery and Molecular Mechanism
    • 10.1021/ar0301781. 15379587
    • Iron-Sulfur Cluster Biosynthesis: Toward an Understanding of Cellular Machinery and Molecular Mechanism. S Mansy JA Cowan, Acc Chem Res 2004 37 719 725 10.1021/ar0301781 15379587
    • (2004) Acc Chem Res , vol.37 , pp. 719-725
    • Mansy, S.1    Cowan, J.A.2
  • 16
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a Scaffold for Iron-Sulfur Cluster Biosynthesis: Sequential Assembly of [2Fe-2S] and [4Fe-4S] Clusters in IscU
    • 10.1021/bi000931n. 10891064
    • IscU as a Scaffold for Iron-Sulfur Cluster Biosynthesis: Sequential Assembly of [2Fe-2S] and [4Fe-4S] Clusters in IscU. JN Agar C Krebs J Frazzon BH Huynh DR Dean MK Johnson, Biochemistry 2000 39 7856 7862 10.1021/bi000931n 10891064
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 18
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • 8464885. 10.1073/pnas.90.7.2754
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. L Zheng RH White VL Cash RF Jack DR Dean, Proc Natl Acad Sci USA 1993 90 2754 2758 8464885 10.1073/pnas.90.7.2754
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 19
    • 24344488420 scopus 로고    scopus 로고
    • Identification of the Mycobacterium tuberculosis SUF machinery as the exclusive mycobacterial system of [Fe-S] cluster assembly: Evidence for its implication in the pathogen's survival
    • 16109955. 10.1128/JB.187.17.6137-6146.2005
    • Identification of the Mycobacterium tuberculosis SUF machinery as the exclusive mycobacterial system of [Fe-S] cluster assembly: evidence for its implication in the pathogen's survival. G Huet M Daffé I Saves, J Bacteriol 2005 187 17 6137 6146 16109955 10.1128/JB.187.17.6137-6146.2005
    • (2005) J Bacteriol , vol.187 , Issue.17 , pp. 6137-6146
    • Huet, G.1    Daffé, M.2    Saves, I.3
  • 20
    • 0037415722 scopus 로고    scopus 로고
    • SufC: An unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
    • 12554644. 10.1093/emboj/cdg061
    • SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. L Nachin L Loiseau D Expert F Barras, EMBO J 2003 22 427 437 12554644 10.1093/emboj/cdg061
    • (2003) EMBO J , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 21
    • 0347991769 scopus 로고    scopus 로고
    • Pathogenic enterococci: New developments in the 21st century
    • 10.1007/s00018-003-3138-0. 14685687
    • Pathogenic enterococci: new developments in the 21st century. PM Tendolkar AS Baghdayan N Shankar, Cell Mol Life Sci 2003 60 2622 2636 10.1007/s00018-003-3138-0 14685687
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2622-2636
    • Tendolkar, P.M.1    Baghdayan, A.S.2    Shankar, N.3
  • 22
    • 1842526422 scopus 로고    scopus 로고
    • Crystal Structure of IscA, an Iron-sulfur Cluster Assembly Protein from Escherichia coli
    • 10.1016/j.jmb.2004.02.027. 15050828
    • Crystal Structure of IscA, an Iron-sulfur Cluster Assembly Protein from Escherichia coli. JR Cupp-Vickery JJ Silberg T Dennis LE Vickery, J Mol Biol 2004 338 127 137 10.1016/j.jmb.2004.02.027 15050828
    • (2004) J Mol Biol , vol.338 , pp. 127-137
    • Cupp-Vickery, J.R.1    Silberg, J.J.2    Dennis, T.3    Vickery, L.E.4
  • 23
    • 27944484814 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli SufA involved in biosynthesis of iron-sulfur clusters: Implications for a functional dimer
    • 10.1016/j.febslet.2005.10.046. 16298366
    • Crystal structure of Escherichia coli SufA involved in biosynthesis of iron-sulfur clusters: implications for a functional dimer. K Wada Y Hasegawa Z Gong Y Minami K Fukuyama Y Takahashi, FEBS Lett 2005 579 29 6543 6548 10.1016/j.febslet.2005.10.046 16298366
    • (2005) FEBS Lett , vol.579 , Issue.29 , pp. 6543-6548
    • Wada, K.1    Hasegawa, Y.2    Gong, Z.3    Minami, Y.4    Fukuyama, K.5    Takahashi, Y.6
  • 24
    • 18844420058 scopus 로고    scopus 로고
    • Structural Characterization of an Iron-Sulfur Cluster Assembly Protein IscU in a Zinc-Bound Form
    • 10.1002/prot.20421. 15815978
    • Structural Characterization of an Iron-Sulfur Cluster Assembly Protein IscU in a Zinc-Bound Form. J Liu N Oganesyan DH Shin J Jancarik H Yokota R Kim SH Kim, Proteins 2005 59 875 881 10.1002/prot.20421 15815978
    • (2005) Proteins , vol.59 , pp. 875-881
    • Liu, J.1    Oganesyan, N.2    Shin, D.H.3    Jancarik, J.4    Yokota, H.5    Kim, R.6    Kim, S.H.7
  • 26
    • 22444449790 scopus 로고    scopus 로고
    • High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf e suggest that all members of the YgdK/Suf e protein family are enhancers of cysteine desulfurases
    • 15930006. 10.1110/ps.041322705
    • High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases. G Liu Z Li Y Chiang T Acton GT Montelione D Murray T Szyperski, Protein Sci 2005 14 6 1597 1608 15930006 10.1110/ps.041322705
    • (2005) Protein Sci , vol.14 , Issue.6 , pp. 1597-1608
    • Liu, G.1    Li, Z.2    Chiang, Y.3    Acton, T.4    Montelione, G.T.5    Murray, D.6    Szyperski, T.7
  • 28
    • 0037077310 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein
    • 10.1074/jbc.M201439200. 11934893
    • Iron-sulfur cluster biosynthesis: Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein. SS Mansy G Wu KK Surerus JA Cowan, J Biol Chem 2002 277 21397 21404 10.1074/jbc.M201439200 11934893
    • (2002) J Biol Chem , vol.277 , pp. 21397-21404
    • Mansy, S.S.1    Wu, G.2    Surerus, K.K.3    Cowan, J.A.4
  • 30
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
    • 10.1074/jbc.M308004200. 12941942
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. FW Outten MJ Wood FM Munoz G Storz, J Biol Chem 2003 278 46 45713 45719 10.1074/jbc.M308004200 12941942
    • (2003) J Biol Chem , vol.278 , Issue.46 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Munoz, F.M.3    Storz, G.4
  • 31
    • 36148932962 scopus 로고    scopus 로고
    • 2+,1+ clusters and functions as a transcriptional repressor of the sufBCDS operon and an autoregulator of sufR in cyanobacteria
    • 10.1074/jbc.M705554200. 17827500
    • 2+,1+ clusters and functions as a transcriptional repressor of the sufBCDS operon and an autoregulator of sufR in cyanobacteria. G Shen R Balasubramanian T Wang Y Wu LM Hoffart C Krebs DA Bryant JH Golbeck, J Biol Chem 2007 282 44 31909 31919 10.1074/jbc.M705554200 17827500
    • (2007) J Biol Chem , vol.282 , Issue.44 , pp. 31909-31919
    • Shen, G.1    Balasubramanian, R.2    Wang, T.3    Wu, Y.4    Hoffart, L.M.5    Krebs, C.6    Bryant, D.A.7    Golbeck, J.H.8
  • 32
    • 1842454714 scopus 로고    scopus 로고
    • Mimicking the action of folding chaperones in molecular dynamics simulations: Application to the refinement of homology-based protein structures
    • 15010545. 10.1110/ps.03449904
    • Mimicking the action of folding chaperones in molecular dynamics simulations: Application to the refinement of homology-based protein structures. H Fan AE Mark, Protein Sci 2004 13 4 992 9 15010545 10.1110/ps.03449904
    • (2004) Protein Sci , vol.13 , Issue.4 , pp. 992-9
    • Fan, H.1    Mark, A.E.2
  • 33
    • 34250192575 scopus 로고    scopus 로고
    • Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein
    • 10.1021/bi6026659. 17506525
    • Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein. K Chandramouli MC Unciuleac S Naik DR Dean BH Huynh MK Johnson, Biochemistry 2007 46 23 6804 6811 10.1021/bi6026659 17506525
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6804-6811
    • Chandramouli, K.1    Unciuleac, M.C.2    Naik, S.3    Dean, D.R.4    Huynh, B.H.5    Johnson, M.K.6
  • 34
    • 51849164641 scopus 로고    scopus 로고
    • Modeling and Molecular Dynamics Simulation of the Human Gonadotropin-Releasing Hormone Receptor in a Lipid Bilayer
    • 10.1021/jp800544x. 18680336
    • Modeling and Molecular Dynamics Simulation of the Human Gonadotropin-Releasing Hormone Receptor in a Lipid Bilayer. E Jardán-Valadez A Ulloa-Aguirre A Pĩeiro, J Phys Chem B 2008 112 34 10704 13 10.1021/jp800544x 18680336
    • (2008) J Phys Chem B , vol.112 , Issue.34 , pp. 10704-13
    • Jardán-Valadez, E.1    Ulloa-Aguirre, A.2    Pĩeiro, A.3
  • 35
    • 58149360795 scopus 로고    scopus 로고
    • Structural refinement of membrane proteins by restrained molecular dynamics and solvent accessibility data
    • 18676641. 10.1529/biophysj.108.142984
    • Structural refinement of membrane proteins by restrained molecular dynamics and solvent accessibility data. P Sompornpisut B Roux E Perozo, Biophys J 95 11 5349 5361 18676641 10.1529/biophysj.108.142984
    • Biophys J , vol.95 , Issue.11 , pp. 5349-5361
    • Sompornpisut, P.1    Roux, B.2    Perozo, E.3
  • 36
    • 27144559598 scopus 로고    scopus 로고
    • Insights into the induced fit mechanism in antithrombin-heparin interaction using molecular dynamics simulations
    • 10.1016/j.jmgm.2005.07.002. 16146701
    • Insights into the induced fit mechanism in antithrombin-heparin interaction using molecular dynamics simulations. H Verli JA Guimarães, J Mol Graph Model 2005 24 3 203 12 10.1016/j.jmgm.2005.07.002 16146701
    • (2005) J Mol Graph Model , vol.24 , Issue.3 , pp. 203-12
    • Verli, H.1    Guimarães, J.A.2
  • 37
    • 33846813813 scopus 로고    scopus 로고
    • Structural and functional behavior of biologically active monomeric melittin
    • 10.1016/j.jmgm.2006.06.006. 16905347
    • Structural and functional behavior of biologically active monomeric melittin. RM Terra JA Guimarães H Verli, J Mol Graph Model 2007 25 6 767 772 10.1016/j.jmgm.2006.06.006 16905347
    • (2007) J Mol Graph Model , vol.25 , Issue.6 , pp. 767-772
    • Terra, R.M.1    Guimarães, J.A.2    Verli, H.3
  • 38
    • 34347227780 scopus 로고    scopus 로고
    • Molecular dynamics analysis of HIV-1 matrix protein: Clarifying differences between crystallographic and solution structures
    • 10.1016/j.jmgm.2006.09.009. 17067836
    • Molecular dynamics analysis of HIV-1 matrix protein: Clarifying differences between crystallographic and solution structures. H Verli A Calazans R Brindeiro A Tanuri JA Guimarães, J Mol Graph Model 2007 26 62 68 10.1016/j.jmgm.2006.09.009 17067836
    • (2007) J Mol Graph Model , vol.26 , pp. 62-68
    • Verli, H.1    Calazans, A.2    Brindeiro, R.3    Tanuri, A.4    Guimarães, J.A.5
  • 39
    • 0037178878 scopus 로고    scopus 로고
    • Hsc66 substrate specificity is directed toward a discrete region of the [Fe-S] cluster template protein IscU
    • 10.1074/jbc.M202814200. 11994302
    • Hsc66 substrate specificity is directed toward a discrete region of the [Fe-S] cluster template protein IscU. KG Hoff DT Ta TL Tapley JJ Silberg LE Vickery, J Biol Chem 2002 277 27353 27359 10.1074/jbc.M202814200 11994302
    • (2002) J Biol Chem , vol.277 , pp. 27353-27359
    • Hoff, K.G.1    Ta, D.T.2    Tapley, T.L.3    Silberg, J.J.4    Vickery, L.E.5
  • 40
    • 33748782301 scopus 로고    scopus 로고
    • HscA and HscB Stimulate [2Fe-2S] Cluster Transfer from IscU to Apoferredoxin in an ATP-Dependent Reaction
    • 16964969. 10.1021/bi061237w
    • HscA and HscB Stimulate [2Fe-2S] Cluster Transfer from IscU to Apoferredoxin in an ATP-Dependent Reaction. K Chandramouli MK Johnson, Biochemistry 2006 45 11087 11095 16964969 10.1021/bi061237w
    • (2006) Biochemistry , vol.45 , pp. 11087-11095
    • Chandramouli, K.1    Johnson, M.K.2
  • 41
    • 0029633168 scopus 로고
    • GROMACS - A message-passing parallel molecular-dynamics implementation
    • 10.1016/0010-4655(95)00042-E
    • GROMACS - a message-passing parallel molecular-dynamics implementation. HJC Berendsen D van der Spoel R van Drunen, Comput Phys Commun 1985 91 43 56 10.1016/0010-4655(95)00042-E
    • (1985) Comput Phys Commun , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Der Van, S.D.2    Van Drunen, R.3
  • 43
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-model and the Swiss-Pdb Viewer: And environment for comparative protein modeling
    • 10.1002/elps.1150181505. 9504803
    • Swiss-model and the Swiss-Pdb Viewer: and environment for comparative protein modeling. N Guex MC Peitsch, Electrophoresis 1997 18 2714 2723 10.1002/elps.1150181505 9504803
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 44
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • 10.1002/bip.360221211. 6667333
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. W Kabsch C Sander, Biopolymers 1983 22 2577 2637 10.1002/bip.360221211 6667333
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 46
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • 10.1063/1.448118
    • Molecular dynamics with coupling to an external bath. HJC Berendsen JPM Postma A DiNola JR Haak, J Chem Phys 1984 81 3684 3690 10.1063/1.448118
    • (1984) J Chem Phys , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Dinola, A.3    Haak, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.