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Volumn 1784, Issue 3, 2008, Pages 543-554

Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G

Author keywords

Antimicrobial peptide; Lactic acid bacteria; Lactococcin G; NMR spectroscopy; Peptide structure

Indexed keywords

BACTERIOCIN; LACTOCOCCIN; LACTOCOCCIN G; POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 42949144745     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.12.002     Document Type: Article
Times cited : (50)

References (69)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 0030974953 scopus 로고    scopus 로고
    • Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action
    • Nissen-Meyer J., and Nes I.F. Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action. Arch. Microbiol. 167 (1997) 67-77
    • (1997) Arch. Microbiol. , vol.167 , pp. 67-77
    • Nissen-Meyer, J.1    Nes, I.F.2
  • 3
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13 (1995) 61-92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 6
    • 28044472548 scopus 로고    scopus 로고
    • Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action
    • Fimland G., Johnsen L., Dalhus B., and Nissen-Meyer J. Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action. J. Pept. Sci. 11 (2005) 688-696
    • (2005) J. Pept. Sci. , vol.11 , pp. 688-696
    • Fimland, G.1    Johnsen, L.2    Dalhus, B.3    Nissen-Meyer, J.4
  • 7
    • 43049094494 scopus 로고    scopus 로고
    • Genetically modified bacteriocins
    • Riley M.A., and Gillor O. (Eds), Horizon Scientific Press
    • Fimland G., and Nissen-Meyer J. Genetically modified bacteriocins. In: Riley M.A., and Gillor O. (Eds). Bacteriocins: Current Research and Applications (2006), Horizon Scientific Press 43-66
    • (2006) Bacteriocins: Current Research and Applications , pp. 43-66
    • Fimland, G.1    Nissen-Meyer, J.2
  • 9
    • 0032005933 scopus 로고    scopus 로고
    • Amphiphilic alpha-helices are important structural motifs in the alpha and beta peptides that constitute the bacteriocin lactococcin G-enhancement of helix formation upon alpha-beta interaction
    • Hauge H.H., Nissen-Meyer J., Nes I.F., and Eijsink V.G. Amphiphilic alpha-helices are important structural motifs in the alpha and beta peptides that constitute the bacteriocin lactococcin G-enhancement of helix formation upon alpha-beta interaction. Eur. J. Biochem. 251 (1998) 565-572
    • (1998) Eur. J. Biochem. , vol.251 , pp. 565-572
    • Hauge, H.H.1    Nissen-Meyer, J.2    Nes, I.F.3    Eijsink, V.G.4
  • 10
    • 0032890798 scopus 로고    scopus 로고
    • Membrane-mimicking entities induce structuring of the two-peptide bacteriocins plantaricin E/F and plantaricin J/K
    • Hauge H.H., Mantzilas D., Eijsink V.G.H., and Nissen-Meyer J. Membrane-mimicking entities induce structuring of the two-peptide bacteriocins plantaricin E/F and plantaricin J/K. J. Bacteriol. 181 (1999) 740-747
    • (1999) J. Bacteriol. , vol.181 , pp. 740-747
    • Hauge, H.H.1    Mantzilas, D.2    Eijsink, V.G.H.3    Nissen-Meyer, J.4
  • 13
    • 0028222975 scopus 로고
    • Kinetic studies of the action of lactacin F, a bacteriocin produced by Lactobacillus johnsonii that forms poration complexes in the cytoplasmic membrane
    • Abee T., Klaenhammer T.R., and Letellier L. Kinetic studies of the action of lactacin F, a bacteriocin produced by Lactobacillus johnsonii that forms poration complexes in the cytoplasmic membrane. Appl. Environ. Microbiol. 60 (1994) 1006-1013
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1006-1013
    • Abee, T.1    Klaenhammer, T.R.2    Letellier, L.3
  • 14
    • 0030921926 scopus 로고    scopus 로고
    • Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor
    • Marciset O., Jeronimus-Stratingh M.C., Mollet B., and Poolman B. Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor. J. Biol. Chem. 272 (1997) 14277-14284
    • (1997) J. Biol. Chem. , vol.272 , pp. 14277-14284
    • Marciset, O.1    Jeronimus-Stratingh, M.C.2    Mollet, B.3    Poolman, B.4
  • 16
    • 0038182634 scopus 로고    scopus 로고
    • Differential roles of the two-component peptides of lactocin 705 in antimicrobial activity
    • Cuozzo S.A., Castellano P., Sesma F.J.M., Vignolo G.M., and Raya R.R. Differential roles of the two-component peptides of lactocin 705 in antimicrobial activity. Curr. Microbiol. 46 (2003) 180-183
    • (2003) Curr. Microbiol. , vol.46 , pp. 180-183
    • Cuozzo, S.A.1    Castellano, P.2    Sesma, F.J.M.3    Vignolo, G.M.4    Raya, R.R.5
  • 17
    • 0026786508 scopus 로고
    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
    • Nissen-Meyer J., Holo H., Håvarstein L.S., Sletten K., and Nes I.F. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J. Bacteriol. 174 (1992) 5686-5692
    • (1992) J. Bacteriol. , vol.174 , pp. 5686-5692
    • Nissen-Meyer, J.1    Holo, H.2    Håvarstein, L.S.3    Sletten, K.4    Nes, I.F.5
  • 18
    • 34248158850 scopus 로고    scopus 로고
    • Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis
    • Oppegård C., Fimland G., Thorbaek L., and Nissen-Meyer J. Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis. Appl. Environ. Microbiol. 73 (2007) 2931-2938
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 2931-2938
    • Oppegård, C.1    Fimland, G.2    Thorbaek, L.3    Nissen-Meyer, J.4
  • 19
    • 0028220778 scopus 로고
    • Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon
    • Allison G.E., Fremaux C., and Klaenhammer T.R. Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J. Bacteriol. 176 (1994) 2235-2241
    • (1994) J. Bacteriol. , vol.176 , pp. 2235-2241
    • Allison, G.E.1    Fremaux, C.2    Klaenhammer, T.R.3
  • 20
    • 0031775980 scopus 로고    scopus 로고
    • Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A
    • Anderssen E.L., Diep D.B., Nes I.F., Eijsink V.G.H., and Nissen-Meyer J. Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A. Appl. Environ. Microbiol. 64 (1998) 2269-2272
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2269-2272
    • Anderssen, E.L.1    Diep, D.B.2    Nes, I.F.3    Eijsink, V.G.H.4    Nissen-Meyer, J.5
  • 21
    • 0034111146 scopus 로고    scopus 로고
    • Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus faecalis BFE 1071
    • Balla E., Dicks L.M.T., du Toit M., van der Merwe M.J., and Holzapfel W.H. Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus faecalis BFE 1071. Appl. Environ. Microbiol. 66 (2000) 1298-1304
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1298-1304
    • Balla, E.1    Dicks, L.M.T.2    du Toit, M.3    van der Merwe, M.J.4    Holzapfel, W.H.5
  • 22
    • 13844256691 scopus 로고    scopus 로고
    • Molecular analysis of the gene cluster involved in the production and secretion of enterocins 1071A and 1071B and of the genes responsible for the replication and transfer of plasmid pEF1071
    • Balla E., and Dicks L.M. Molecular analysis of the gene cluster involved in the production and secretion of enterocins 1071A and 1071B and of the genes responsible for the replication and transfer of plasmid pEF1071. Int. J. Food Microbiol. 99 (2005) 33-45
    • (2005) Int. J. Food Microbiol. , vol.99 , pp. 33-45
    • Balla, E.1    Dicks, L.M.2
  • 23
    • 0034656248 scopus 로고    scopus 로고
    • Identification and nucleotide sequence of genes involved in the synthesis of lactocin 705, a two-peptide bacteriocin from Lactobacillus casei CRL 705
    • Cuozzo S.A., Sesma F., Palacios J.M., de Ruiz Holgado A.P., and Raya R.R. Identification and nucleotide sequence of genes involved in the synthesis of lactocin 705, a two-peptide bacteriocin from Lactobacillus casei CRL 705. FEMS Microbiol. Lett. 185 (2000) 157-161
    • (2000) FEMS Microbiol. Lett. , vol.185 , pp. 157-161
    • Cuozzo, S.A.1    Sesma, F.2    Palacios, J.M.3    de Ruiz Holgado, A.P.4    Raya, R.R.5
  • 24
    • 0029772572 scopus 로고    scopus 로고
    • Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11
    • Diep D.B., Håvarstein L.S., and Nes I.F. Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J. Bacteriol. 178 (1996) 4472-4483
    • (1996) J. Bacteriol. , vol.178 , pp. 4472-4483
    • Diep, D.B.1    Håvarstein, L.S.2    Nes, I.F.3
  • 25
    • 0036230805 scopus 로고    scopus 로고
    • Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. salivarius UCC118
    • Flynn S., van Sinderen D., Thornton G.M., Holo H., Nes I.F., and Collins J.K. Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. salivarius UCC118. Microbiology 148 (2002) 973-984
    • (2002) Microbiology , vol.148 , pp. 973-984
    • Flynn, S.1    van Sinderen, D.2    Thornton, G.M.3    Holo, H.4    Nes, I.F.5    Collins, J.K.6
  • 27
    • 0036589172 scopus 로고    scopus 로고
    • Two-peptide bacteriocins produced by lactic acid bacteria
    • Garneau S., Martin N.I., and Vederas J.C. Two-peptide bacteriocins produced by lactic acid bacteria. Biochimie 84 (2002) 577-592
    • (2002) Biochimie , vol.84 , pp. 577-592
    • Garneau, S.1    Martin, N.I.2    Vederas, J.C.3
  • 28
    • 0028789406 scopus 로고
    • Purification and partial amino acid sequence of plantaricin S, a bacteriocin produced by Lactobacillus plantarum LPCO10, the activity of which depends on the complementary action of two peptides
    • Jimenez-Diaz R., Ruiz-Barba J.L., Cathcart D.P., Holo H., Nes I.F., Sletten K.H., and Warner P.J. Purification and partial amino acid sequence of plantaricin S, a bacteriocin produced by Lactobacillus plantarum LPCO10, the activity of which depends on the complementary action of two peptides. Appl. Environ. Microbiol. 61 (1995) 4459-4463
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4459-4463
    • Jimenez-Diaz, R.1    Ruiz-Barba, J.L.2    Cathcart, D.P.3    Holo, H.4    Nes, I.F.5    Sletten, K.H.6    Warner, P.J.7
  • 29
    • 0037224719 scopus 로고    scopus 로고
    • Purification and genetic characterization of plantaricin NC8, a novel coculture-inducible two-peptide bacteriocin from Lactobacillus plantarum NC8
    • Maldonado A., Ruiz-Barba J.L., and Jimenez-Diaz R. Purification and genetic characterization of plantaricin NC8, a novel coculture-inducible two-peptide bacteriocin from Lactobacillus plantarum NC8. Appl. Environ. Microbiol. 69 (2003) 383-389
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 383-389
    • Maldonado, A.1    Ruiz-Barba, J.L.2    Jimenez-Diaz, R.3
  • 30
    • 0031767742 scopus 로고    scopus 로고
    • Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754
    • McCormick J.K., Poon A., Sailer M., Gao Y., Roy K.L., McMullen L.M., Vederas J.C., Stiles M.E., and Van Belkum M.J. Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754. Appl. Environ. Microbiol. 64 (1998) 4757-4766
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4757-4766
    • McCormick, J.K.1    Poon, A.2    Sailer, M.3    Gao, Y.4    Roy, K.L.5    McMullen, L.M.6    Vederas, J.C.7    Stiles, M.E.8    Van Belkum, M.J.9
  • 31
    • 0035172918 scopus 로고    scopus 로고
    • The group I strain of Streptococcus mutans, UA140, produces both the lantibiotic mutacin I and a nonlantibiotic bacteriocin, mutacin IV
    • Qi F.X., Chen P., and Caufield P.W. The group I strain of Streptococcus mutans, UA140, produces both the lantibiotic mutacin I and a nonlantibiotic bacteriocin, mutacin IV. Appl. Environ. Microbiol. 67 (2001) 15-21
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 15-21
    • Qi, F.X.1    Chen, P.2    Caufield, P.W.3
  • 34
    • 33646544691 scopus 로고    scopus 로고
    • Lactococcin Q, a novel two-peptide bacteriocin produced by Lactococcus lactis QU 4
    • Zendo T., Koga S., Shigeri Y., Nakayama J., and Sonomoto K. Lactococcin Q, a novel two-peptide bacteriocin produced by Lactococcus lactis QU 4. Appl. Environ. Microbiol. 72 (2006) 3383-3389
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3383-3389
    • Zendo, T.1    Koga, S.2    Shigeri, Y.3    Nakayama, J.4    Sonomoto, K.5
  • 37
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • Fregeau Gallagher N.L., Sailer M., Niemczura W.P., Nakashima T.T., Stiles M.E., and Vederas J.C. Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria. Biochemistry 36 (1997) 15062-15072
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Fregeau Gallagher, N.L.1    Sailer, M.2    Niemczura, W.P.3    Nakashima, T.T.4    Stiles, M.E.5    Vederas, J.C.6
  • 38
    • 0033598699 scopus 로고    scopus 로고
    • Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria
    • Wang Y.J., Henz M.E., Gallagher N.L.F., Chai S.Y., Gibbs A.C., Yan L.Z., Stiles M.E., Wishart D.S., and Vederas J.C. Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria. Biochemistry 38 (1999) 15438-15447
    • (1999) Biochemistry , vol.38 , pp. 15438-15447
    • Wang, Y.J.1    Henz, M.E.2    Gallagher, N.L.F.3    Chai, S.Y.4    Gibbs, A.C.5    Yan, L.Z.6    Stiles, M.E.7    Wishart, D.S.8    Vederas, J.C.9
  • 39
    • 0141817944 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridges
    • Uteng M., Hauge H.H., Markwick P.R.L., Fimland G., Mantzilas D., Nissen-Meyer J., and Muhle-Goll C. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridges. Biochemistry 42 (2003) 11417-11426
    • (2003) Biochemistry , vol.42 , pp. 11417-11426
    • Uteng, M.1    Hauge, H.H.2    Markwick, P.R.L.3    Fimland, G.4    Mantzilas, D.5    Nissen-Meyer, J.6    Muhle-Goll, C.7
  • 40
    • 28944447119 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A
    • Haugen H.S., Fimland G., Nissen-Meyer J., and Kristiansen P.E. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A. Biochemistry 44 (2005) 16149-16157
    • (2005) Biochemistry , vol.44 , pp. 16149-16157
    • Haugen, H.S.1    Fimland, G.2    Nissen-Meyer, J.3    Kristiansen, P.E.4
  • 42
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
    • Huth J.R., Bewley C.A., Jackson B.M., Hinnebusch A.G., Clore G.M., and Gronenborn A.M. Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci. 6 (1997) 2359-2364
    • (1997) Protein Sci. , vol.6 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3    Hinnebusch, A.G.4    Clore, G.M.5    Gronenborn, A.M.6
  • 43
    • 0037731254 scopus 로고    scopus 로고
    • A rapid method to attain isotope labeled small soluble peptides for NMR studies
    • Koenig B.W., Rogowski M., and Louis J.M. A rapid method to attain isotope labeled small soluble peptides for NMR studies. J. Biomol. NMR 26 (2003) 193-202
    • (2003) J. Biomol. NMR , vol.26 , pp. 193-202
    • Koenig, B.W.1    Rogowski, M.2    Louis, J.M.3
  • 44
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley J., Lu M., and Bracken C. A method for efficient isotopic labeling of recombinant proteins. J. Biomol. NMR 20 (2001) 71-75
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 45
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 46
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz J.M., Qian H., York E.J., Stewart J.M., and Baldwin R.L. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers 31 (1991) 1463-1470
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 47
    • 44049118259 scopus 로고
    • Experiments for recording pure-absorption heteronuclear correlation spectra using pulsed field gradients
    • Davis A.L., Keeler J., Laue E.D., and Moskau D. Experiments for recording pure-absorption heteronuclear correlation spectra using pulsed field gradients. J. Magn. Reson. 98 (1992) 207-216
    • (1992) J. Magn. Reson. , vol.98 , pp. 207-216
    • Davis, A.L.1    Keeler, J.2    Laue, E.D.3    Moskau, D.4
  • 48
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • Palmer III A.G., Cavanagh J., Wright P.E., and Rance M. Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J. Magn. Reson. 93 (1991) 151-170
    • (1991) J. Magn. Reson. , vol.93 , pp. 151-170
    • Palmer III, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 49
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L., Keifer P., and Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114 (1992) 10663-10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.1    Keifer, P.2    Saarinen, T.3
  • 51
    • 0343359244 scopus 로고
    • Investigation of exchange processes by 2-dimensional NMR-spectroscopy
    • Jeener J., Meier B.H., Bachmann P., and Ernst R.R. Investigation of exchange processes by 2-dimensional NMR-spectroscopy. J. Chem. Phys. 71 (1979) 4546-4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 53
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: application to proton correlation spectroscopy
    • Braunschweiler L., and Ernst R.R. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53 (1983) 521-528
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 54
    • 0026890433 scopus 로고
    • Measurement of two-bond JCOH alpha coupling constants in proteins uniformly enriched with 13C
    • Vuister G.W., and Bax A. Measurement of two-bond JCOH alpha coupling constants in proteins uniformly enriched with 13C. J. Biomol. NMR 2 (1992) 401-405
    • (1992) J. Biomol. NMR , vol.2 , pp. 401-405
    • Vuister, G.W.1    Bax, A.2
  • 58
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 59
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 60
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T., Guntert P., and Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319 (2002) 209-227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 61
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 62
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods
    • Sreerama N., and Woody R.W. Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 242 (1994) 497-507
    • (1994) J. Mol. Biol. , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 63
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N., and Woody R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209 (1993) 32-44
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 64
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson W.C. Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins 35 (1999) 307-312
    • (1999) Proteins , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 65
    • 0025943469 scopus 로고
    • Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy
    • Wishart D.S., Sykes B.D., and Richards F.M. Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy. FEBS Lett. 293 (1991) 72-80
    • (1991) FEBS Lett. , vol.293 , pp. 72-80
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 66
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D.S., Sykes B.D., and Richards F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222 (1991) 311-333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 67
    • 0037338558 scopus 로고    scopus 로고
    • Purification and characterization of brochocin A and brochocin B (10-43), a functional fragment generated by heterologous expression in Carnobacterium piscicola
    • Garneau S., Ference C.A., van Belkum M.J., Stiles M.E., and Vederas J.C. Purification and characterization of brochocin A and brochocin B (10-43), a functional fragment generated by heterologous expression in Carnobacterium piscicola. Appl. Environ. Microbiol. 69 (2003) 1352-1358
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1352-1358
    • Garneau, S.1    Ference, C.A.2    van Belkum, M.J.3    Stiles, M.E.4    Vederas, J.C.5
  • 68
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs
    • Senes A., Engel D.E., and DeGrado W.F. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 14 (2004) 465-479
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 69
    • 33847796246 scopus 로고    scopus 로고
    • Common mechanisms of target cell recognition and immunity for class II bacteriocins
    • Diep D.B., Skaugen M., Salehian Z., Holo H., and Nes I.F. Common mechanisms of target cell recognition and immunity for class II bacteriocins. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 2384-2389
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2384-2389
    • Diep, D.B.1    Skaugen, M.2    Salehian, Z.3    Holo, H.4    Nes, I.F.5


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