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Volumn 394, Issue 4, 2009, Pages 718-731

NanC Crystal Structure, a Model for Outer-Membrane Channels of the Acidic Sugar-Specific KdgM Porin Family

Author keywords

crystal structure; KdgM family; outer membrane channel; sialic acid

Indexed keywords

NANC PROTEIN; OLIGOSACCHARIDE; OUTER MEMBRANE PROTEIN; PORIN; SIALIC ACID; UNCLASSIFIED DRUG;

EID: 70449533002     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.09.054     Document Type: Article
Times cited : (35)

References (67)
  • 1
    • 0141585145 scopus 로고    scopus 로고
    • Solute uptake through general porins
    • Delcour A.H. Solute uptake through general porins. Front. Biosci. 8 (2003) 1055-1071
    • (2003) Front. Biosci. , vol.8 , pp. 1055-1071
    • Delcour, A.H.1
  • 2
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67 (2003) 593-656
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 3
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., and Welte W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282 (1998) 2215-2220
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 4
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss M.S., Abele U., Weckesser J., Welte W., Schiltz E., and Schulz G.E. Molecular architecture and electrostatic properties of a bacterial porin. Science 254 (1991) 1627-1630
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schulz, G.E.6
  • 5
    • 0028153088 scopus 로고
    • Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus
    • Kreusch A., and Schulz G.E. Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus. J. Mol. Biol. 243 (1994) 891-905
    • (1994) J. Mol. Biol. , vol.243 , pp. 891-905
    • Kreusch, A.1    Schulz, G.E.2
  • 7
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E. coli porins
    • Cowan S.W., Schirmer T., Rummel G., Steiert M., Ghosh R., Pauptit R.A., et al. Crystal structures explain functional properties of two E. coli porins. Nature 358 (1992) 727-733
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Schirmer, T.2    Rummel, G.3    Steiert, M.4    Ghosh, R.5    Pauptit, R.A.6
  • 8
    • 0033560795 scopus 로고    scopus 로고
    • Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae
    • Dutzler R., Rummel G., Alberti S., Hernandez-Alles S., Phale P., Rosenbusch J., et al. Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae. Structure 7 (1999) 425-434
    • (1999) Structure , vol.7 , pp. 425-434
    • Dutzler, R.1    Rummel, G.2    Alberti, S.3    Hernandez-Alles, S.4    Phale, P.5    Rosenbusch, J.6
  • 9
    • 0034665240 scopus 로고    scopus 로고
    • Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 Å resolution
    • Zeth K., Diederichs K., Welte W., and Engelhardt H. Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 Å resolution. Structure 8 (2000) 981-992
    • (2000) Structure , vol.8 , pp. 981-992
    • Zeth, K.1    Diederichs, K.2    Welte, W.3    Engelhardt, H.4
  • 10
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • Forst D., Welte W., Wacker T., and Diederichs K. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nat. Struct. Biol. 5 (1998) 37-46
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 11
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer T., Keller T.A., Wang Y.F., and Rosenbusch J.P. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267 (1995) 512-514
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 12
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer J.E., Hofnung M., and Schulz G.E. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol. 266 (1997) 761-775
    • (1997) J. Mol. Biol. , vol.266 , pp. 761-775
    • Meyer, J.E.1    Hofnung, M.2    Schulz, G.E.3
  • 14
    • 46049091548 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protein OpdK from Pseudomonas aeruginosa
    • Biswas S., Mohammad M.M., Movileanu L., and van den Berg B. Crystal structure of the outer membrane protein OpdK from Pseudomonas aeruginosa. Structure 16 (2008) 1027-1035
    • (2008) Structure , vol.16 , pp. 1027-1035
    • Biswas, S.1    Mohammad, M.M.2    Movileanu, L.3    van den Berg, B.4
  • 15
    • 33846113922 scopus 로고    scopus 로고
    • An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane
    • Moraes T.F., Bains M., Hancock R.E., and Strynadka N.C. An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Nat. Struct. Mol. Biol. 14 (2007) 85-87
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 85-87
    • Moraes, T.F.1    Bains, M.2    Hancock, R.E.3    Strynadka, N.C.4
  • 17
    • 4444258925 scopus 로고    scopus 로고
    • Crystal structure of the bacterial nucleoside transporter Tsx
    • Ye J., and van den Berg B. Crystal structure of the bacterial nucleoside transporter Tsx. EMBO J. 23 (2004) 3187-3195
    • (2004) EMBO J. , vol.23 , pp. 3187-3195
    • Ye, J.1    van den Berg, B.2
  • 18
    • 33745727012 scopus 로고    scopus 로고
    • Crystal structure of the monomeric porin OmpG
    • Subbarao G.V., and van den Berg B. Crystal structure of the monomeric porin OmpG. J. Mol. Biol. 360 (2006) 750-759
    • (2006) J. Mol. Biol. , vol.360 , pp. 750-759
    • Subbarao, G.V.1    van den Berg, B.2
  • 19
    • 33747623998 scopus 로고    scopus 로고
    • Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation
    • Yildiz O., Vinothkumar K.R., Goswami P., and Kuhlbrandt W. Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. EMBO J. 25 (2006) 3702-3713
    • (2006) EMBO J. , vol.25 , pp. 3702-3713
    • Yildiz, O.1    Vinothkumar, K.R.2    Goswami, P.3    Kuhlbrandt, W.4
  • 20
    • 2642522855 scopus 로고    scopus 로고
    • Crystal structure of the long-chain fatty acid transporter FadL
    • van den Berg B., Black P.N., Clemons Jr. W.M., and Rapoport T.A. Crystal structure of the long-chain fatty acid transporter FadL. Science 304 (2004) 1506-1509
    • (2004) Science , vol.304 , pp. 1506-1509
    • van den Berg, B.1    Black, P.N.2    Clemons Jr., W.M.3    Rapoport, T.A.4
  • 21
    • 47249160634 scopus 로고    scopus 로고
    • Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation
    • Hearn E.M., Patel D.R., and van den Berg B. Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation. Proc. Natl Acad. Sci. USA 105 (2008) 8601-8606
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 8601-8606
    • Hearn, E.M.1    Patel, D.R.2    van den Berg, B.3
  • 22
    • 0038000585 scopus 로고    scopus 로고
    • Topology of the Erwinia chrysanthemi oligogalacturonate porin KdgM
    • Pellinen T., Ahlfors H., Blot N., and Condemine G. Topology of the Erwinia chrysanthemi oligogalacturonate porin KdgM. Biochem. J. 372 (2003) 329-334
    • (2003) Biochem. J. , vol.372 , pp. 329-334
    • Pellinen, T.1    Ahlfors, H.2    Blot, N.3    Condemine, G.4
  • 23
    • 0037040884 scopus 로고    scopus 로고
    • The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family
    • Blot N., Berrier C., Hugouvieux-Cotte-Pattat N., Ghazi A., and Condemine G. The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family. J. Biol. Chem. 277 (2002) 7936-7944
    • (2002) J. Biol. Chem. , vol.277 , pp. 7936-7944
    • Blot, N.1    Berrier, C.2    Hugouvieux-Cotte-Pattat, N.3    Ghazi, A.4    Condemine, G.5
  • 24
    • 9144270620 scopus 로고    scopus 로고
    • Comparative genomics of the KdgR regulon in Erwinia chrysanthemi 3937 and other gamma-proteobacteria
    • Rodionov D.A., Gelfand M.S., and Hugouvieux-Cotte-Pattat N. Comparative genomics of the KdgR regulon in Erwinia chrysanthemi 3937 and other gamma-proteobacteria. Microbiology 150 (2004) 3571-3590
    • (2004) Microbiology , vol.150 , pp. 3571-3590
    • Rodionov, D.A.1    Gelfand, M.S.2    Hugouvieux-Cotte-Pattat, N.3
  • 25
    • 34547735489 scopus 로고    scopus 로고
    • Differential regulation of two oligogalacturonate outer membrane channels, KdgN and KdgM, of Dickeya dadantii (Erwinia chrysanthemi)
    • Condemine G., and Ghazi A. Differential regulation of two oligogalacturonate outer membrane channels, KdgN and KdgM, of Dickeya dadantii (Erwinia chrysanthemi). J. Bacteriol. 189 (2007) 5955-5962
    • (2007) J. Bacteriol. , vol.189 , pp. 5955-5962
    • Condemine, G.1    Ghazi, A.2
  • 26
    • 14644401707 scopus 로고    scopus 로고
    • Function and expression of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli
    • Condemine G., Berrier C., Plumbridge J., and Ghazi A. Function and expression of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli. J. Bacteriol. 187 (2005) 1959-1965
    • (2005) J. Bacteriol. , vol.187 , pp. 1959-1965
    • Condemine, G.1    Berrier, C.2    Plumbridge, J.3    Ghazi, A.4
  • 27
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective
    • Angata T., and Varki A. Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective. Chem. Rev. 102 (2002) 439-469
    • (2002) Chem. Rev. , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 29
    • 9244264945 scopus 로고    scopus 로고
    • Integrated regulatory responses of fimB to N-acetylneuraminic (sialic) acid and GlcNAc in Escherichia coli K-12
    • Sohanpal B.K., El-Labany S., Lahooti M., Plumbridge J.A., and Blomfield I.C. Integrated regulatory responses of fimB to N-acetylneuraminic (sialic) acid and GlcNAc in Escherichia coli K-12. Proc. Natl Acad. Sci. USA 101 (2004) 16322-16327
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 16322-16327
    • Sohanpal, B.K.1    El-Labany, S.2    Lahooti, M.3    Plumbridge, J.A.4    Blomfield, I.C.5
  • 30
    • 33846597207 scopus 로고    scopus 로고
    • Multiple co-regulatory elements and IHF are necessary for the control of fimB expression in response to sialic acid and N-acetylglucosamine in Escherichia coli K-12
    • Sohanpal B.K., Friar S., Roobol J., Plumbridge J.A., and Blomfield I.C. Multiple co-regulatory elements and IHF are necessary for the control of fimB expression in response to sialic acid and N-acetylglucosamine in Escherichia coli K-12. Mol. Microbiol. 63 (2007) 1223-1236
    • (2007) Mol. Microbiol. , vol.63 , pp. 1223-1236
    • Sohanpal, B.K.1    Friar, S.2    Roobol, J.3    Plumbridge, J.A.4    Blomfield, I.C.5
  • 32
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • Schulz G.E. The structure of bacterial outer membrane proteins. Biochim. Biophys. Acta 1565 (2002) 308-317
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 35
    • 0027640084 scopus 로고
    • Bacterial porins: structure and function
    • Schulz G.E. Bacterial porins: structure and function. Curr. Opin. Cell Biol. 5 (1993) 701-707
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 701-707
    • Schulz, G.E.1
  • 36
    • 0027998871 scopus 로고
    • Intramolecular self-cleavage of polysialic acid
    • Manzi A.E., Higa H.H., Diaz S., and Varki A. Intramolecular self-cleavage of polysialic acid. J. Biol. Chem. 269 (1994) 23617-23624
    • (1994) J. Biol. Chem. , vol.269 , pp. 23617-23624
    • Manzi, A.E.1    Higa, H.H.2    Diaz, S.3    Varki, A.4
  • 37
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler R., Wang Y.F., Rizkallah P., Rosenbusch J.P., and Schirmer T. Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4 (1996) 127-134
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.F.2    Rizkallah, P.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 39
    • 0019824138 scopus 로고
    • Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli
    • Nikaido H., and Rosenberg E.Y. Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli. J. Gen. Physiol. 77 (1981) 121-135
    • (1981) J. Gen. Physiol. , vol.77 , pp. 121-135
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 40
    • 0020597554 scopus 로고
    • Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins
    • Nikaido H., and Rosenberg E.Y. Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins. J. Bacteriol. 153 (1983) 241-252
    • (1983) J. Bacteriol. , vol.153 , pp. 241-252
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 42
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., and Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22 (2006) 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 43
    • 0029992419 scopus 로고    scopus 로고
    • From acids to osmZ: multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli
    • Pratt L.A., Hsing W., Gibson K.E., and Silhavy T.J. From acids to osmZ: multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli. Mol. Microbiol. 20 (1996) 911-917
    • (1996) Mol. Microbiol. , vol.20 , pp. 911-917
    • Pratt, L.A.1    Hsing, W.2    Gibson, K.E.3    Silhavy, T.J.4
  • 44
    • 0033579482 scopus 로고    scopus 로고
    • Brownian dynamics simulation of ion flow through porin channels
    • Schirmer T., and Phale P.S. Brownian dynamics simulation of ion flow through porin channels. J. Mol. Biol. 294 (1999) 1159-1167
    • (1999) J. Mol. Biol. , vol.294 , pp. 1159-1167
    • Schirmer, T.1    Phale, P.S.2
  • 45
    • 44949192066 scopus 로고    scopus 로고
    • Structural biology of pectin degradation by Enterobacteriaceae
    • Abbott D.W., and Boraston A.B. Structural biology of pectin degradation by Enterobacteriaceae. Microbiol. Mol. Biol. Rev. 72 (2008) 301-316
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 301-316
    • Abbott, D.W.1    Boraston, A.B.2
  • 47
    • 0041528535 scopus 로고    scopus 로고
    • Distant cis-active sequences and sialic acid control the expression of fimB in Escherichia coli K-12
    • El-Labany S., Sohanpal B.K., Lahooti M., Akerman R., and Blomfield I.C. Distant cis-active sequences and sialic acid control the expression of fimB in Escherichia coli K-12. Mol. Microbiol. 49 (2003) 1109-1118
    • (2003) Mol. Microbiol. , vol.49 , pp. 1109-1118
    • El-Labany, S.1    Sohanpal, B.K.2    Lahooti, M.3    Akerman, R.4    Blomfield, I.C.5
  • 48
    • 33846104333 scopus 로고    scopus 로고
    • Temporal gene-expression in Escherichia coli K-12 biofilms
    • Domka J., Lee J., Bansal T., and Wood T.K. Temporal gene-expression in Escherichia coli K-12 biofilms. Environ. Microbiol. 9 (2007) 332-346
    • (2007) Environ. Microbiol. , vol.9 , pp. 332-346
    • Domka, J.1    Lee, J.2    Bansal, T.3    Wood, T.K.4
  • 49
    • 0032102987 scopus 로고    scopus 로고
    • Coupling site-directed mutagenesis with high-level expression: large scale production of mutant porins from E. coli
    • Prilipov A., Phale P.S., Van Gelder P., Rosenbusch J.P., and Koebnik R. Coupling site-directed mutagenesis with high-level expression: large scale production of mutant porins from E. coli. FEMS Microbiol. Lett. 163 (1998) 65-72
    • (1998) FEMS Microbiol. Lett. , vol.163 , pp. 65-72
    • Prilipov, A.1    Phale, P.S.2    Van Gelder, P.3    Rosenbusch, J.P.4    Koebnik, R.5
  • 52
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 54
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0
    • Bricogne G., Vonrhein C., Flensburg C., Schiltz M., and Paciorek W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr., Sect. D: Biol. Crystallogr. 59 (2003) 2023-2030
    • (2003) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 55
  • 59
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
    • Davis I.W., Leaver-Fay A., Chen V.B., Block J.N., Kapral G.J., Wang X., et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35 (2007) 375-383
    • (2007) Nucleic Acids Res. , vol.35 , pp. 375-383
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5    Wang, X.6
  • 61
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 62
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct., Funct., Genet. 11 (1991) 281-296
    • (1991) Proteins: Struct., Funct., Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 64
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell Jr. A.D., Feig M., and Brooks III C.L. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25 (2004) 1400-1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 65
    • 0141956090 scopus 로고    scopus 로고
    • Generalized born model with a simple smoothing function
    • Im W., Lee M.S., and Brooks III C.L. Generalized born model with a simple smoothing function. J. Comput. Chem. 24 (2003) 1691-1702
    • (2003) J. Comput. Chem. , vol.24 , pp. 1691-1702
    • Im, W.1    Lee, M.S.2    Brooks III, C.L.3
  • 66
    • 0242322528 scopus 로고    scopus 로고
    • An implicit membrane generalized Born theory for the study of structure, stability, and interactions of membrane proteins
    • Im W., Feig M., and Brooks III C.L. An implicit membrane generalized Born theory for the study of structure, stability, and interactions of membrane proteins. Biophys. J. 85 (2003) 2900-2918
    • (2003) Biophys. J. , vol.85 , pp. 2900-2918
    • Im, W.1    Feig, M.2    Brooks III, C.L.3
  • 67
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints-molecular dynamics of n-alkanes
    • Ryckaert J.P., Ciccotti G., and Berendsen H.J.C. Numerical integration of the Cartesian equations of motion of a system with constraints-molecular dynamics of n-alkanes. J. Comput. Phys. 23 (1977) 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3


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