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Volumn 25, Issue 2, 2007, Pages 48-55

Immobilisation of proteins by atomic clusters on surfaces

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHEMISORPTION; ENZYME IMMOBILIZATION; NANOTECHNOLOGY; SURFACE PHENOMENA;

EID: 33846185527     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2006.12.004     Document Type: Article
Times cited : (33)

References (46)
  • 1
    • 18144378483 scopus 로고    scopus 로고
    • Gas-phase catalysis by atomic and cluster metal ions: The ultimate single-site catalysts
    • Bohme D., and Schwarz H. Gas-phase catalysis by atomic and cluster metal ions: The ultimate single-site catalysts. Angew. Chem. Int. Ed. Engl. 44 (2005) 2336-2354
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 2336-2354
    • Bohme, D.1    Schwarz, H.2
  • 2
    • 13444310873 scopus 로고    scopus 로고
    • Materials produced by assembling gas-phase nanoclusters
    • Binns C. Materials produced by assembling gas-phase nanoclusters. Curr. Opin. Solid State Mater. Sci. 8 (2004) 203-209
    • (2004) Curr. Opin. Solid State Mater. Sci. , vol.8 , pp. 203-209
    • Binns, C.1
  • 3
    • 0742321804 scopus 로고    scopus 로고
    • Gold nanoparticles: Assembly, supramolecular chemistry, quantum-size-related properties, and applications toward biology, catalysis, and nanotechnology
    • Daniel M., and Astruc D. Gold nanoparticles: Assembly, supramolecular chemistry, quantum-size-related properties, and applications toward biology, catalysis, and nanotechnology. Chem. Rev. 104 (2004) 293-346
    • (2004) Chem. Rev. , vol.104 , pp. 293-346
    • Daniel, M.1    Astruc, D.2
  • 4
    • 33645084516 scopus 로고    scopus 로고
    • Nanotechnologies in proteomics
    • Ivanov Y., et al. Nanotechnologies in proteomics. Proteomics 6 (2006) 1399-1414
    • (2006) Proteomics , vol.6 , pp. 1399-1414
    • Ivanov, Y.1
  • 5
    • 10044258525 scopus 로고    scopus 로고
    • Integrated nanoparticle-biomolecule hybrid systems: Synthesis, properties, and applications
    • Katz E., and Willner I. Integrated nanoparticle-biomolecule hybrid systems: Synthesis, properties, and applications. Angew. Chem. Int. Ed. Engl. 43 (2004) 6042-6108
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 6042-6108
    • Katz, E.1    Willner, I.2
  • 6
    • 0038143185 scopus 로고    scopus 로고
    • Nanotechnology: convergence with modern biology and medicine
    • Roco M. Nanotechnology: convergence with modern biology and medicine. Curr. Opin. Biotechnol. 14 (2003) 337-346
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 337-346
    • Roco, M.1
  • 7
    • 0036977748 scopus 로고    scopus 로고
    • Ordered nanoparticle arrays formed on engineered chaperonin protein templates
    • McMillan R.A., et al. Ordered nanoparticle arrays formed on engineered chaperonin protein templates. Nat. Mater. 1 (2002) 247-252
    • (2002) Nat. Mater. , vol.1 , pp. 247-252
    • McMillan, R.A.1
  • 8
    • 0037497251 scopus 로고    scopus 로고
    • Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles
    • Ishii D., et al. Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles. Nature 423 (2003) 628-632
    • (2003) Nature , vol.423 , pp. 628-632
    • Ishii, D.1
  • 9
    • 24644523590 scopus 로고    scopus 로고
    • Microarray-based detection of protein binding and functionality by gold nanoparticle probes
    • Wang Z., et al. Microarray-based detection of protein binding and functionality by gold nanoparticle probes. Anal. Chem. 77 (2005) 5770-5774
    • (2005) Anal. Chem. , vol.77 , pp. 5770-5774
    • Wang, Z.1
  • 10
    • 0041494363 scopus 로고    scopus 로고
    • Biological applications of colloidal nanocrystals
    • Parak W., et al. Biological applications of colloidal nanocrystals. Nanotechnology 14 (2003) R15-R27
    • (2003) Nanotechnology , vol.14
    • Parak, W.1
  • 11
    • 23844558083 scopus 로고    scopus 로고
    • Quantum dots as cellular probes
    • Alivisatos A., et al. Quantum dots as cellular probes. Annu. Rev. Biomed. Eng. 7 (2005) 55-76
    • (2005) Annu. Rev. Biomed. Eng. , vol.7 , pp. 55-76
    • Alivisatos, A.1
  • 12
    • 0037039370 scopus 로고    scopus 로고
    • Molecular immunolabeling with recombinant single-chain variable fragment (scFv) antibodies designed with metal-binding domains
    • Malecki M., et al. Molecular immunolabeling with recombinant single-chain variable fragment (scFv) antibodies designed with metal-binding domains. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 213-218
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 213-218
    • Malecki, M.1
  • 13
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu H., et al. Global analysis of protein activities using proteome chips. Science 293 (2001) 2101-2105
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1
  • 14
    • 0012522653 scopus 로고    scopus 로고
    • Protein chips: from concept to practice
    • Lee Y.S., and Mrksich M. Protein chips: from concept to practice. Trends Biotechnol. 20 (2002) S14-S18
    • (2002) Trends Biotechnol. , vol.20
    • Lee, Y.S.1    Mrksich, M.2
  • 15
    • 0012618901 scopus 로고
    • Atomic force microscope
    • Binnig G., et al. Atomic force microscope. Phys. Rev. Lett. 56 (1986) 930-933
    • (1986) Phys. Rev. Lett. , vol.56 , pp. 930-933
    • Binnig, G.1
  • 16
    • 4344704617 scopus 로고    scopus 로고
    • The native architecture of a photosynthetic membrane
    • Bahatyrova S., et al. The native architecture of a photosynthetic membrane. Nature 430 (2004) 1058-1062
    • (2004) Nature , vol.430 , pp. 1058-1062
    • Bahatyrova, S.1
  • 17
    • 0034713072 scopus 로고    scopus 로고
    • Structural biology - proton-powered turbine of a plant motor
    • Seelert H., et al. Structural biology - proton-powered turbine of a plant motor. Nature 405 (2000) 418-419
    • (2000) Nature , vol.405 , pp. 418-419
    • Seelert, H.1
  • 18
    • 0037468835 scopus 로고    scopus 로고
    • Hidden complexity in the mechanical properties of titin
    • Williams P.M., et al. Hidden complexity in the mechanical properties of titin. Nature 422 (2003) 446-449
    • (2003) Nature , vol.422 , pp. 446-449
    • Williams, P.M.1
  • 19
    • 0034321268 scopus 로고    scopus 로고
    • Pinning of size-selected Ag clusters on graphite surfaces
    • Carroll S.J., et al. Pinning of size-selected Ag clusters on graphite surfaces. J. Chem. Phys. 113 (2000) 7723-7727
    • (2000) J. Chem. Phys. , vol.113 , pp. 7723-7727
    • Carroll, S.J.1
  • 20
    • 33644936250 scopus 로고    scopus 로고
    • Pinning of size-selected gold and nickel nanoclusters on graphite
    • Di Vece M., et al. Pinning of size-selected gold and nickel nanoclusters on graphite. Phys. Rev. B (2005) 72
    • (2005) Phys. Rev. B , pp. 72
    • Di Vece, M.1
  • 21
    • 17644394570 scopus 로고    scopus 로고
    • Size-selected cluster beam source based on radio frequency magnetron plasma sputtering and gas condensation
    • Pratontep S., et al. Size-selected cluster beam source based on radio frequency magnetron plasma sputtering and gas condensation. Rev. Sci. Instrum. 76 (2005) 045103
    • (2005) Rev. Sci. Instrum. , vol.76 , pp. 045103
    • Pratontep, S.1
  • 22
    • 0000386138 scopus 로고    scopus 로고
    • A new high transmission infinite range mass selector for cluster and nanoparticle beams
    • von Issendorff B., and Palmer R.E. A new high transmission infinite range mass selector for cluster and nanoparticle beams. Rev. Sci. Instrum. 70 (1999) 4497-4501
    • (1999) Rev. Sci. Instrum. , vol.70 , pp. 4497-4501
    • von Issendorff, B.1    Palmer, R.E.2
  • 23
    • 15744365701 scopus 로고    scopus 로고
    • High-temperature stability of size-selected gold nanoclusters pinned on graphite
    • Yin T., et al. High-temperature stability of size-selected gold nanoclusters pinned on graphite. Adv. Mater. 17 (2005) 731-734
    • (2005) Adv. Mater. , vol.17 , pp. 731-734
    • Yin, T.1
  • 24
    • 0042766190 scopus 로고    scopus 로고
    • Nanostructured surfaces from size-selected clusters
    • Palmer R.E., et al. Nanostructured surfaces from size-selected clusters. Nat. Mater. 2 (2003) 443-448
    • (2003) Nat. Mater. , vol.2 , pp. 443-448
    • Palmer, R.E.1
  • 25
    • 1642415729 scopus 로고    scopus 로고
    • Clusters for biology: immobilisation of proteins by size-selected metal clusters
    • Collins J.A., et al. Clusters for biology: immobilisation of proteins by size-selected metal clusters. Appl. Surf. Sci. 226 (2004) 197-208
    • (2004) Appl. Surf. Sci. , vol.226 , pp. 197-208
    • Collins, J.A.1
  • 26
    • 1542375064 scopus 로고    scopus 로고
    • Immobilisation of protein molecules by size-selected metal clusters on surfaces
    • Leung C., et al. Immobilisation of protein molecules by size-selected metal clusters on surfaces. Adv. Mater. 16 (2004) 223-226
    • (2004) Adv. Mater. , vol.16 , pp. 223-226
    • Leung, C.1
  • 27
    • 33645325206 scopus 로고    scopus 로고
    • Residue-specific immobilization of protein molecules by size-selected clusters
    • Prisco U., et al. Residue-specific immobilization of protein molecules by size-selected clusters. J. R. Soc. Interface 2 (2005) 169-175
    • (2005) J. R. Soc. Interface , vol.2 , pp. 169-175
    • Prisco, U.1
  • 28
    • 0344584910 scopus 로고    scopus 로고
    • Conformational changes in the plasma protein fibrinogen upon adsorption to graphite and mica investigated by atomic force microscopy
    • Marchin K.L., and Berrie C.L. Conformational changes in the plasma protein fibrinogen upon adsorption to graphite and mica investigated by atomic force microscopy. Langmuir 19 (2003) 9883-9888
    • (2003) Langmuir , vol.19 , pp. 9883-9888
    • Marchin, K.L.1    Berrie, C.L.2
  • 29
    • 0037905447 scopus 로고    scopus 로고
    • Direct observation of antifreeze glycoprotein-fraction 8 on hydrophobic and hydrophilic interfaces using atomic force microscopy
    • Sarno D.M., et al. Direct observation of antifreeze glycoprotein-fraction 8 on hydrophobic and hydrophilic interfaces using atomic force microscopy. Langmuir 19 (2003) 4740-4744
    • (2003) Langmuir , vol.19 , pp. 4740-4744
    • Sarno, D.M.1
  • 30
    • 0037197254 scopus 로고    scopus 로고
    • Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature
    • Tsodikov O.V., et al. Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature. J. Comput. Chem. 23 (2002) 600-609
    • (2002) J. Comput. Chem. , vol.23 , pp. 600-609
    • Tsodikov, O.V.1
  • 31
    • 0033199270 scopus 로고    scopus 로고
    • Array biosensor for simultaneous identification of bacterial, viral, and protein analytes
    • Rowe C.A., et al. Array biosensor for simultaneous identification of bacterial, viral, and protein analytes. Anal. Chem. 71 (1999) 3846-3852
    • (1999) Anal. Chem. , vol.71 , pp. 3846-3852
    • Rowe, C.A.1
  • 32
    • 0036199649 scopus 로고    scopus 로고
    • Peptide chips for the quantitative evaluation of protein kinase activity
    • Houseman B.T., et al. Peptide chips for the quantitative evaluation of protein kinase activity. Nat. Biotechnol. 20 (2002) 270-274
    • (2002) Nat. Biotechnol. , vol.20 , pp. 270-274
    • Houseman, B.T.1
  • 33
    • 0038631903 scopus 로고    scopus 로고
    • Protein assembly by orthogonal chemical ligation methods
    • Nilsson B.L., et al. Protein assembly by orthogonal chemical ligation methods. J. Am. Chem. Soc. 125 (2003) 5268-5269
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5268-5269
    • Nilsson, B.L.1
  • 34
    • 0242692373 scopus 로고    scopus 로고
    • Current status of protein chip development in terms of fabrication and application
    • Seong S.Y., and Choi C.Y. Current status of protein chip development in terms of fabrication and application. Proteomics 3 (2003) 2176-2189
    • (2003) Proteomics , vol.3 , pp. 2176-2189
    • Seong, S.Y.1    Choi, C.Y.2
  • 35
    • 21044443738 scopus 로고    scopus 로고
    • Protein-detecting microarrays: Current accomplishments and requirements
    • Tomizaki K.Y., et al. Protein-detecting microarrays: Current accomplishments and requirements. Chembiochem. 6 (2005) 783-799
    • (2005) Chembiochem. , vol.6 , pp. 783-799
    • Tomizaki, K.Y.1
  • 36
    • 32044444587 scopus 로고    scopus 로고
    • Recent advances of protein microarrays
    • Hultschig C., et al. Recent advances of protein microarrays. Curr. Opin. Chem. Biol. 10 (2006) 4-10
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 4-10
    • Hultschig, C.1
  • 37
    • 30444437914 scopus 로고    scopus 로고
    • Fluorescence enhancement by metal-core/silica-shell nanoparticles
    • Tovmachenko O.G., et al. Fluorescence enhancement by metal-core/silica-shell nanoparticles. Adv. Mater. 18 (2006) 91-95
    • (2006) Adv. Mater. , vol.18 , pp. 91-95
    • Tovmachenko, O.G.1
  • 38
    • 0043192619 scopus 로고    scopus 로고
    • Preparing protein microarrays by soft-landing of mass-selected ions
    • Ouyang Z., et al. Preparing protein microarrays by soft-landing of mass-selected ions. Science 301 (2003) 1351-1354
    • (2003) Science , vol.301 , pp. 1351-1354
    • Ouyang, Z.1
  • 39
    • 33644905549 scopus 로고    scopus 로고
    • Electrospray ion beam deposition of clusters and biomolecules
    • Rauschenbach S., et al. Electrospray ion beam deposition of clusters and biomolecules. Small 2 (2006) 540-547
    • (2006) Small , vol.2 , pp. 540-547
    • Rauschenbach, S.1
  • 40
    • 0001240711 scopus 로고    scopus 로고
    • Trapping of size-selected Ag clusters at surface steps
    • Carroll S.J., et al. Trapping of size-selected Ag clusters at surface steps. Appl. Phys. Lett. 72 (1998) 305-307
    • (1998) Appl. Phys. Lett. , vol.72 , pp. 305-307
    • Carroll, S.J.1
  • 41
    • 0037422939 scopus 로고    scopus 로고
    • Scaling relations for implantation of size-selected Au, Ag, and Si clusters into graphite
    • Pratontep S., et al. Scaling relations for implantation of size-selected Au, Ag, and Si clusters into graphite. Phys. Rev. Lett. 90 (2003) 055503. http://prl.aps.org/
    • (2003) Phys. Rev. Lett. , vol.90 , pp. 055503
    • Pratontep, S.1
  • 42
    • 17644394570 scopus 로고    scopus 로고
    • Size-selected cluster beam source based on radio frequency magnetron plasma sputtering and gas condensation
    • 045103.01-045103.09
    • Pratontep S., et al. Size-selected cluster beam source based on radio frequency magnetron plasma sputtering and gas condensation. Rev. Sci. Instrum. 76 (2005). http://rsi.aip.org/rsi 045103.01-045103.09
    • (2005) Rev. Sci. Instrum. , vol.76
    • Pratontep, S.1
  • 43
    • 0015222647 scopus 로고
    • Interpretation of protein structures - estimation of static accessibility
    • Lee B., and Richards F.M. Interpretation of protein structures - estimation of static accessibility. J. Mol. Biol. 55 (1971) 379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 44
    • 0017429069 scopus 로고
    • Areas, volumes, packing, and protein-structure
    • Richards F.M. Areas, volumes, packing, and protein-structure. Annu. Rev. Biophys. Bioeng. 6 (1977) 151-176
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 45
    • 0035933058 scopus 로고    scopus 로고
    • Quantification of the hydrophobic interaction by simulations of the aggregation of small hydrophobic solutes in water
    • Raschke T.M., et al. Quantification of the hydrophobic interaction by simulations of the aggregation of small hydrophobic solutes in water. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 5965-5969
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 5965-5969
    • Raschke, T.M.1
  • 46
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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