메뉴 건너뛰기




Volumn 3, Issue 1, 2013, Pages 149-160

Periplasmic binding proteins in thermophiles: Characterization and potential application of an arginine-binding protein from Thermotoga maritima: A brief thermo-story

Author keywords

ABC transporters; Arginine; Periplasmic binding proteins; Structural stability; Unfolding

Indexed keywords


EID: 84894297392     PISSN: None     EISSN: 20751729     Source Type: Journal    
DOI: 10.3390/life3010149     Document Type: Review
Times cited : (13)

References (46)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C.F. ABC transporters: From microorganisms to man. Annu. Rev. Cell Biol. 1992, 8, 67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 1842610700 scopus 로고    scopus 로고
    • The ABC transporter structure and mechanism: Perspectives on recent research
    • Jones, P.M.; George, A.M. The ABC transporter structure and mechanism: Perspectives on recent research. Cell Mol. Life Sci. 2004, 61, 682-699.
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 682-699
    • Jones, P.M.1    George, A.M.2
  • 3
    • 34247123807 scopus 로고    scopus 로고
    • Structure and function of ABC transporters
    • Linton, K.J. Structure and function of ABC transporters. Physiology 2007, 22, 122-130.
    • (2007) Physiology , vol.22 , pp. 122-130
    • Linton, K.J.1
  • 5
    • 70349312287 scopus 로고    scopus 로고
    • The ATP-binding cassette family: A structural perspective
    • Kos, V.; Ford, R.C. The ATP-binding cassette family: a structural perspective. Cell Mol. Life Sci. 2009, 66, 3111-3126.
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 3111-3126
    • Kos, V.1    Ford, R.C.2
  • 6
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson, A.L.; Dassa, E.; Orelle, C.; Chen, J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 2008, 72, 317-364.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 9
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham, M.L.; Khare, D.; Quiocho, F.A.; Davidson, A.L.; Chen, J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 2007, 450, 515-521.
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 10
    • 0024198129 scopus 로고
    • Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma
    • Gilson, E.; Alloing, G.; Schmidt, T.; Claverys, J.P.; Dudler, R.; Hofnung, M. Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma. EMBO J. 1988, 7, 3971-3974.
    • (1988) EMBO J. , vol.7 , pp. 3971-3974
    • Gilson, E.1    Alloing, G.2    Schmidt, T.3    Claverys, J.P.4    Dudler, R.5    Hofnung, M.6
  • 11
    • 0031037399 scopus 로고    scopus 로고
    • Amino acid transport in taxonomically diverse cyanobacteria and identification of two genes encoding elements of a neutral amino acid permease putatively involved in recapture of leaked hydrophobic amino acids
    • Montesinos, M.L.; Herrero, A.; Flores, E. Amino acid transport in taxonomically diverse cyanobacteria and identification of two genes encoding elements of a neutral amino acid permease putatively involved in recapture of leaked hydrophobic amino acids. J. Bacteriol. 1997, 179, 853-862.
    • (1997) J. Bacteriol. , vol.179 , pp. 853-862
    • Montesinos, M.L.1    Herrero, A.2    Flores, E.3
  • 12
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F.A.; Ledvina, P.S. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol. Microbiol. 1996, 20, 17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 13
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R.; Saier, M.H., Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993, 57, 320-346.
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier Jr., M.H.2
  • 14
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: A versatile superfamily for protein engineering
    • Dwyer, M.A.; Hellinga, H.W. Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr. Opin. Struct. Biol. 2004, 14, 495-504.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 15
    • 0033548125 scopus 로고    scopus 로고
    • Domain dislocation: A change of core structure in periplasmic binding proteins in their evolutionary history
    • Fukami-Kobayashi, K.; Tateno, Y.; Nishikawa, K. Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history. J. Mol. Biol. 1999, 286, 279-290.
    • (1999) J. Mol. Biol. , vol.286 , pp. 279-290
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 16
    • 0036209769 scopus 로고    scopus 로고
    • The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation
    • Lee, Y.H.; Dorwart, M.R.; Hazlett, K.R.; Deka, R.K.; Norgard, M.V.; Radolf, J.D.; Hasemann, C.A. The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation. J. Bacteriol. 2002, 184, 2300-2304.
    • (2002) J. Bacteriol. , vol.184 , pp. 2300-2304
    • Lee, Y.H.1    Dorwart, M.R.2    Hazlett, K.R.3    Deka, R.K.4    Norgard, M.V.5    Radolf, J.D.6    Hasemann, C.A.7
  • 17
    • 0037424465 scopus 로고    scopus 로고
    • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding
    • Karpowich, N.K.; Huang, H.H.; Smith, P.C.; Hunt, J.F. Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding. J. Biol. Chem. 2003, 278, 8429-8434.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 18
    • 0029074899 scopus 로고
    • A third periplasmic transport system for L-arginine in Escherichia coli: Molecular characterization of the artPIQMJ genes, arginine binding and transport
    • Wissenbach, U.; Six, S.; Bongaerts, J.; Ternes, D.; Steinwachs, S.; Unden, G. A third periplasmic transport system for L-arginine in Escherichia coli: molecular characterization of the artPIQMJ genes, arginine binding and transport. Mol. Microbiol. 1995, 17, 675-686.
    • (1995) Mol. Microbiol. , vol.17 , pp. 675-686
    • Wissenbach, U.1    Six, S.2    Bongaerts, J.3    Ternes, D.4    Steinwachs, S.5    Unden, G.6
  • 19
    • 79958772445 scopus 로고    scopus 로고
    • Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351
    • Stamp, A.L.; Owen, P.; El Omari, K.; Lockyer, M.; Lamb, H.K.; Charles, I.G.; Hawkins, A.R.; Stammers, D.K. Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351. Proteins 2011, 79, 2352-2357.
    • (2011) Proteins , vol.79 , pp. 2352-2357
    • Stamp, A.L.1    Owen, P.2    El Omari, K.3    Lockyer, M.4    Lamb, H.K.5    Charles, I.G.6    Hawkins, A.R.7    Stammers, D.K.8
  • 20
    • 0027235488 scopus 로고
    • Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand
    • Oh, B.H.; Pandit, J.; Kang, C.H.; Nikaido, K.; Gokcen, S.; Ames, G.F.; Kim, S.H. Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. J. Biol. Chem. 1993, 268, 11348-11355.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11348-11355
    • Oh, B.H.1    Pandit, J.2    Kang, C.H.3    Nikaido, K.4    Gokcen, S.5    Ames, G.F.6    Kim, S.H.7
  • 21
    • 0031660549 scopus 로고    scopus 로고
    • Phosphorylation of the periplasmic binding protein in two transport systems for arginine incorporation in Escherichia coli K-12 is unrelated to the function of the transport system
    • Celis, R.T.; Leadlay, P.F.; Roy, I.; Hansen, A. Phosphorylation of the periplasmic binding protein in two transport systems for arginine incorporation in Escherichia coli K-12 is unrelated to the function of the transport system. J. Bacteriol. 1998, 180, 4828-4833.
    • (1998) J. Bacteriol. , vol.180 , pp. 4828-4833
    • Celis, R.T.1    Leadlay, P.F.2    Roy, I.3    Hansen, A.4
  • 22
    • 0034039993 scopus 로고    scopus 로고
    • Ligand-binding proteins: Their potential for application in systems for controlled delivery and uptake of ligands
    • De Wolf, F.A.; Brett, G.M. Ligand-binding proteins: their potential for application in systems for controlled delivery and uptake of ligands. Pharmacol. Rev. 2000, 52, 207-236.
    • (2000) Pharmacol. Rev. , vol.52 , pp. 207-236
    • De Wolf, F.A.1    Brett, G.M.2
  • 23
    • 80052535969 scopus 로고    scopus 로고
    • Arginase I deficiency: Severe infantile presentation with hyperammonemia: More common than reported?
    • Jain-Ghai, S.; Nagamani, S.C.; Blaser, S.; Siriwardena, K.; Feigenbaum, A. Arginase I deficiency: severe infantile presentation with hyperammonemia: more common than reported? Mol. Genet. Metab. 2011, 104, 107-111.
    • (2011) Mol. Genet. Metab. , vol.104 , pp. 107-111
    • Jain-Ghai, S.1    Nagamani, S.C.2    Blaser, S.3    Siriwardena, K.4    Feigenbaum, A.5
  • 24
    • 0001878491 scopus 로고
    • Urea cycle enzymes
    • In Scriver, C.R., Beaudet, A.L., Sly, W.S., Valle, D., Eds.; McGraw-Hill: New York, NY, USA
    • Brusilov, S.W.; Horwich, A.L. Urea cycle enzymes. In The Metabolic Basis of Inherited Disease; Scriver, C.R., Beaudet, A.L., Sly, W.S., Valle, D., Eds.; McGraw-Hill: New York, NY, USA, 1989; pp 629-663.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 629-663
    • Brusilov, S.W.1    Horwich, A.L.2
  • 25
    • 0001599370 scopus 로고
    • Role of endothelium-derived nitric oxide in the regulation of blood pressure
    • Rees, D.D.; Palmer, R.M.; Moncada, S. Role of endothelium-derived nitric oxide in the regulation of blood pressure. Proc. Natl. Acad. Sci. USA 1989, 86, 3375-3378.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3375-3378
    • Rees, D.D.1    Palmer, R.M.2    Moncada, S.3
  • 26
    • 0033813512 scopus 로고    scopus 로고
    • Does ADMA cause endothelial dysfunction?
    • Cooke, J.P. Does ADMA cause endothelial dysfunction? Arterioscler. Thromb. Vasc. Biol. 2000, 20, 2032-2037.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 2032-2037
    • Cooke, J.P.1
  • 27
    • 0024428094 scopus 로고
    • Effects of endothelium-derived nitric oxide on peripheral arteriolar tone in man
    • Vallance, P.; Collier, J.; Moncada, S. Effects of endothelium-derived nitric oxide on peripheral arteriolar tone in man. Lancet 1989, 2, 997-1000.
    • (1989) Lancet , vol.2 , pp. 997-1000
    • Vallance, P.1    Collier, J.2    Moncada, S.3
  • 28
    • 0035311988 scopus 로고    scopus 로고
    • Optical determination of glutamine using a genetically engineered protein
    • Dattelbaum, J.D.; Lakowicz, J.R. Optical determination of glutamine using a genetically engineered protein. Anal. Biochem. 2001, 291, 89-95.
    • (2001) Anal. Biochem. , vol.291 , pp. 89-95
    • Dattelbaum, J.D.1    Lakowicz, J.R.2
  • 29
    • 35648996014 scopus 로고    scopus 로고
    • Engineering and rapid selection of a low-affinity glucose/galactose-binding protein for a glucose biosensor
    • Amiss, T.J.; Sherman, D.B.; Nycz, C.M.; Andaluz, S.A.; Pitner, J.B. Engineering and rapid selection of a low-affinity glucose/galactose-binding protein for a glucose biosensor. Protein Sci. 2007, 16, 2350-2359.
    • (2007) Protein Sci. , vol.16 , pp. 2350-2359
    • Amiss, T.J.1    Sherman, D.B.2    Nycz, C.M.3    Andaluz, S.A.4    Pitner, J.B.5
  • 30
    • 29244431641 scopus 로고    scopus 로고
    • Glucose biosensors as models for the development of advanced protein-based biosensors
    • Staiano, M.; Bazzicalupo, P.; Rossi, M.; D'Auria, S. Glucose biosensors as models for the development of advanced protein-based biosensors. Mol. Biosyst. 2005, 1, 354-362.
    • (2005) Mol. Biosyst. , vol.1 , pp. 354-362
    • Staiano, M.1    Bazzicalupo, P.2    Rossi, M.3    D'Auria, S.4
  • 31
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °C
    • Huber, R.; Langworthy, T.A.; König, H.; Thomm, M.; Woese, C.R.; Sleytr, U.B.; Stetter, K.O. Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °C. Arch. Microbiol. 1986, 144, 324-333.
    • (1986) Arch. Microbiol. , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    König, H.3    Thomm, M.4    Woese, C.R.5    Sleytr, U.B.6    Stetter, K.O.7
  • 33
    • 0034141421 scopus 로고    scopus 로고
    • Structural analysis of DNA sequence: Evidence for lateral gene transfer in Thermotoga maritima
    • Worning, P.; Jensen, L.J.; Nelson, K.E.; Brunak, S.; Ussery, D.W. Structural analysis of DNA sequence: evidence for lateral gene transfer in Thermotoga maritima. Nucleic Acids Res. 2000, 28, 706-709.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 706-709
    • Worning, P.1    Jensen, L.J.2    Nelson, K.E.3    Brunak, S.4    Ussery, D.W.5
  • 34
    • 34748917914 scopus 로고    scopus 로고
    • Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein
    • Tian, Y.; Cuneo, M.J.; Changela, A.; Hocker, B.; Beese, L.S.; Hellinga, H.W. Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein. Protein Sci. 2007, 16, 2240-2250.
    • (2007) Protein Sci. , vol.16 , pp. 2240-2250
    • Tian, Y.1    Cuneo, M.J.2    Changela, A.3    Hocker, B.4    Beese, L.S.5    Hellinga, H.W.6
  • 35
    • 0037468510 scopus 로고    scopus 로고
    • Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers
    • Fox, J.D.; Routzahn, K.M.; Bucher, M.H.; Waugh, D.S. Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers. FEBS Lett. 2003, 537, 53-57.
    • (2003) FEBS Lett. , vol.537 , pp. 53-57
    • Fox, J.D.1    Routzahn, K.M.2    Bucher, M.H.3    Waugh, D.S.4
  • 36
    • 33144472334 scopus 로고    scopus 로고
    • Several archaeal homologs of putative oligopeptide-binding proteins encoded by Thermotoga maritima bind sugars
    • Nanavati, D.M.; Thirangoon, K.; Noll, K.M. Several archaeal homologs of putative oligopeptide-binding proteins encoded by Thermotoga maritima bind sugars. Appl Environ. Microbiol. 2006, 72, 1336-1345.
    • (2006) Appl Environ. Microbiol. , vol.72 , pp. 1336-1345
    • Nanavati, D.M.1    Thirangoon, K.2    Noll, K.M.3
  • 37
    • 72949100493 scopus 로고    scopus 로고
    • Amino acid transport in thermophiles: Characterization of an arginine-binding protein in Thermotoga maritima
    • Luchansky, M.S.; Der, B.S.; D'Auria, S.; Pocsfalvi, G.; Iozzino, L.; Marasco, D.; Dattelbaum, J.D. Amino acid transport in thermophiles: characterization of an arginine-binding protein in Thermotoga maritima. Mol. Biosyst. 2010, 6, 142-151.
    • (2010) Mol. Biosyst. , vol.6 , pp. 142-151
    • Luchansky, M.S.1    Der, B.S.2    D'Auria, S.3    Pocsfalvi, G.4    Iozzino, L.5    Marasco, D.6    Dattelbaum, J.D.7
  • 38
    • 0032562651 scopus 로고    scopus 로고
    • The structure of glutamine-binding protein complexed with glutamine at 1.94 A resolution: Comparisons with other amino acid binding proteins
    • Sun, Y.J.; Rose, J.; Wang, B.C.; Hsiao, C.D. The structure of glutamine-binding protein complexed with glutamine at 1.94 A resolution: Comparisons with other amino acid binding proteins. J. Mol. Biol. 1998, 278, 219-229.
    • (1998) J. Mol. Biol. , vol.278 , pp. 219-229
    • Sun, Y.J.1    Rose, J.2    Wang, B.C.3    Hsiao, C.D.4
  • 39
    • 57749104100 scopus 로고    scopus 로고
    • Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport
    • Cuneo, M.J.; Changela, A.; Miklos, A.E.; Beese, L.S.; Krueger, J.K.; Hellinga, H.W. Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport. J. Biol. Chem. 2008, 283, 32812-32820.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32812-32820
    • Cuneo, M.J.1    Changela, A.2    Miklos, A.E.3    Beese, L.S.4    Krueger, J.K.5    Hellinga, H.W.6
  • 40
    • 34047164005 scopus 로고    scopus 로고
    • Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for-keto acid binding
    • doi:10.1186/1472-6807-7-11
    • Gonin, S.; Arnoux, P.; Pierru, B.; Lavergne, J.; Alonso, B.; Sabaty, M.; Pignol, D. Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for-keto acid binding. BMC Struct. Biol. 2007, doi:10.1186/1472-6807-7-11.
    • (2007) BMC Struct. Biol.
    • Gonin, S.1    Arnoux, P.2    Pierru, B.3    Lavergne, J.4    Alonso, B.5    Sabaty, M.6    Pignol, D.7
  • 41
    • 33846963817 scopus 로고    scopus 로고
    • A bacterial arginine-agmatine exchange transporter involved in extreme acid resistance
    • Fang, Y.; Kolmakova-Partensky, L.; Miller, C. A bacterial arginine-agmatine exchange transporter involved in extreme acid resistance. J. Biol. Chem. 2007, 282, 176-182.
    • (2007) J. Biol. Chem. , vol.282 , pp. 176-182
    • Fang, Y.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 42
    • 77949742907 scopus 로고    scopus 로고
    • Amino acid transport in thermophiles: Characterization of an arginine-binding protein in Thermotoga maritima. 2. Molecular organization and structural stability
    • Scire, A.; Marabotti, A.; Staiano, M.; Iozzino, L.; Luchansky, M.S.; Der, B.S.; Dattelbaum, J.D.; Tanfani, F.; D'Auria, S. Amino acid transport in thermophiles: characterization of an arginine-binding protein in Thermotoga maritima. 2. Molecular organization and structural stability. Mol. Biosyst. 2010, 6, 687-698.
    • (2010) Mol. Biosyst. , vol.6 , pp. 687-698
    • Scire, A.1    Marabotti, A.2    Staiano, M.3    Iozzino, L.4    Luchansky, M.S.5    Der, B.S.6    Dattelbaum, J.D.7    Tanfani, F.8    D'Auria, S.9
  • 43
    • 36549063540 scopus 로고    scopus 로고
    • Crystal structures and mutational analysis of the arginine-, lysine-, histidine-binding protein ArtJ from Geobacillus stearothermophilus. Implications for interactions of ArtJ with its cognate ATP-binding cassette transporter, Art(MP)2
    • Vahedi-Faridi, A.; Eckey, V.; Scheffel, F.; Alings, C.; Landmesser, H.; Schneider, E.; Saenger, W. Crystal structures and mutational analysis of the arginine-, lysine-, histidine-binding protein ArtJ from Geobacillus stearothermophilus. Implications for interactions of ArtJ with its cognate ATP-binding cassette transporter, Art(MP)2. J. Mol. Biol. 2008, 375, 448-459.
    • (2008) J. Mol. Biol. , vol.375 , pp. 448-459
    • Vahedi-Faridi, A.1    Eckey, V.2    Scheffel, F.3    Alings, C.4    Landmesser, H.5    Schneider, E.6    Saenger, W.7
  • 44
    • 0030595368 scopus 로고    scopus 로고
    • The crystal structure of glutamine-binding protein from Escherichia coli
    • Hsiao, C.D.; Sun, Y.J.; Rose, J.; Wang, B.C. The crystal structure of glutamine-binding protein from Escherichia coli. J. Mol. Biol. 1996, 262, 225-242.
    • (1996) J. Mol. Biol. , vol.262 , pp. 225-242
    • Hsiao, C.D.1    Sun, Y.J.2    Rose, J.3    Wang, B.C.4
  • 45
    • 84894296725 scopus 로고    scopus 로고
    • Amino acid transport in thermophiles: Characterization of an arginine-binding protein from Thermotoga maritima. 3. Conformational dynamics and stability
    • in press
    • Ausili, A.; Pennacchio, A.; Staiano, M.; Dattelbaum, J.D.; Fessas, D.; Schiraldi, A.; D'Auria, S. Amino acid transport in thermophiles: Characterization of an arginine-binding protein from Thermotoga maritima. 3. Conformational dynamics and stability. J. Photochem. Photobiol. B 2012, in press.
    • (2012) J. Photochem. Photobiol. B
    • Ausili, A.1    Pennacchio, A.2    Staiano, M.3    Dattelbaum, J.D.4    Fessas, D.5    Schiraldi, A.6    D'Auria, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.